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Conserved domains on  [gi|426398029|ref|XP_004065205|]
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coagulation factor VIII isoform X1 [Gorilla gorilla gorilla]

Protein Classification

CuRO_1_FVIII_like and CuRO_3_FVIII_like domain-containing protein( domain architecture ID 10199334)

protein containing domains CuRO_1_FVIII_like, CuRO_3_FVIII_like, CuRO_5_FVIII_like, and CuRO_6_FVIII_like

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 399-575 5.04e-115

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: 361.94  E-value: 5.04e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  399 KTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGD 478
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  479 TLLIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINM 558
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 426398029  559 ERDLASGLIGPLLICYK 575
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-201 2.62e-110

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: 348.12  E-value: 2.62e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   22 RRYYLGAVELSWDYMQSDLGELPVDarfpprvPKSFPFNTSVVYKKTVFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYD 101
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGDPASE-------QRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  102 TVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHV 181
Cdd:cd14452    74 TVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQV 153

                         170       180
                  ....*....|....*....|
gi 426398029  182 DLVKDLNSGLIGALLVCREG 201
Cdd:cd14452   154 DPVKDVNSGLIGALLVCRMG 173
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1714-1880 1.17e-102

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: 326.07  E-value: 1.17e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1714 TRHYFIAAVERLWDYGMSSSPHVLR----NRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDN 1789
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPQHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1790 IMVTFKNQASRPYSFYSSLISYEEDQRqgAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSG 1869
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQR--AEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSG 158

                         170
                  ....*....|.
gi 426398029 1870 LIGPLLVCHTN 1880
Cdd:cd04228   159 LIGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1892-2035 1.54e-95

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: 304.50  E-value: 1.54e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1892 VQEFALFFTIFDETRSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNEN 1971
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 426398029 1972 IHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 588-730 1.64e-88

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: 284.45  E-value: 1.64e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  588 DKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDF 667
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029  668 LSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSC 730
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 211-345 1.18e-80

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: 261.76  E-value: 1.18e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  211 LHKFILLFAVFDEGKSWHSETKNSLMQDRdAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIFL 290
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRDK-FKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 426398029  291 EGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKV 345
Cdd:cd11015    80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2195-2344 1.49e-58

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: 198.73  E-value: 1.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 2195 MPLGMESKAiSDAQITASSYFTnmfATWSPSKARLHlqgRSNAWRPQVNNPKEWLQVDFQKTMKVTGITTQGVKSLLTSM 2274
Cdd:cd00057     1 EPLGMESGL-ADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSE 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 2275 YVKEFLISSSQDGHHWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWMHQIALRMEVLG 2344
Cdd:cd00057    74 WVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2042-2187 1.95e-53

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: 184.09  E-value: 1.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 2042 TPLGMASGHiRDFQITASGQYG-QWAPKLARLHysgSINAWSTKE--PFSWIKVDLLAPMIIHGIKTQGARQKFSSLYIS 2118
Cdd:cd00057     1 EPLGMESGL-ADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVT 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 426398029 2119 QFIIMYSLDGKKWQTYRGNstGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMG 2187
Cdd:cd00057    77 SYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
 
Name Accession Description Interval E-value
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 399-575 5.04e-115

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: 361.94  E-value: 5.04e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  399 KTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGD 478
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  479 TLLIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINM 558
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 426398029  559 ERDLASGLIGPLLICYK 575
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-201 2.62e-110

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: 348.12  E-value: 2.62e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   22 RRYYLGAVELSWDYMQSDLGELPVDarfpprvPKSFPFNTSVVYKKTVFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYD 101
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGDPASE-------QRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  102 TVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHV 181
Cdd:cd14452    74 TVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQV 153

                         170       180
                  ....*....|....*....|
gi 426398029  182 DLVKDLNSGLIGALLVCREG 201
Cdd:cd14452   154 DPVKDVNSGLIGALLVCRMG 173
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1714-1880 1.17e-102

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: 326.07  E-value: 1.17e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1714 TRHYFIAAVERLWDYGMSSSPHVLR----NRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDN 1789
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPQHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1790 IMVTFKNQASRPYSFYSSLISYEEDQRqgAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSG 1869
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQR--AEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSG 158

                         170
                  ....*....|.
gi 426398029 1870 LIGPLLVCHTN 1880
Cdd:cd04228   159 LIGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1892-2035 1.54e-95

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: 304.50  E-value: 1.54e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1892 VQEFALFFTIFDETRSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNEN 1971
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 426398029 1972 IHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 588-730 1.64e-88

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: 284.45  E-value: 1.64e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  588 DKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDF 667
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029  668 LSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSC 730
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 211-345 1.18e-80

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: 261.76  E-value: 1.18e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  211 LHKFILLFAVFDEGKSWHSETKNSLMQDRdAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIFL 290
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRDK-FKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 426398029  291 EGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKV 345
Cdd:cd11015    80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2195-2344 1.49e-58

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: 198.73  E-value: 1.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 2195 MPLGMESKAiSDAQITASSYFTnmfATWSPSKARLHlqgRSNAWRPQVNNPKEWLQVDFQKTMKVTGITTQGVKSLLTSM 2274
Cdd:cd00057     1 EPLGMESGL-ADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSE 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 2275 YVKEFLISSSQDGHHWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWMHQIALRMEVLG 2344
Cdd:cd00057    74 WVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2042-2187 1.95e-53

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: 184.09  E-value: 1.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 2042 TPLGMASGHiRDFQITASGQYG-QWAPKLARLHysgSINAWSTKE--PFSWIKVDLLAPMIIHGIKTQGARQKFSSLYIS 2118
Cdd:cd00057     1 EPLGMESGL-ADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVT 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 426398029 2119 QFIIMYSLDGKKWQTYRGNstGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMG 2187
Cdd:cd00057    77 SYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2039-2188 7.21e-40

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: 144.96  E-value: 7.21e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   2039 KCQTPLGMASghirDFQITASGQYgqWAPKLARLHYsGSINAWSTKEP--FSWIKVDLLAPMIIHGIKTQGArqkFSSLY 2116
Cdd:smart00231    1 PCNEPLGLES----DSQITASSSY--WAAKIARLNG-GSDGGWCPAKNdlPPWIQVDLGRLRTVTGVITGRR---HGNGD 70

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 426398029   2117 ISQFIIMYSLDGKKWQTYRGnstGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGC 2188
Cdd:smart00231   71 WVTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2192-2345 4.11e-33

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: 125.70  E-value: 4.11e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   2192 SCSMPLGMESkaisDAQITASSyftnmfATWSPSKARLHlQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGITTQGVKSLL 2271
Cdd:smart00231    1 PCNEPLGLES----DSQITASS------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 426398029   2272 TsmYVKEFLISSSqDGHHWTlFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWMHQIALRMEVLGC 2345
Cdd:smart00231   70 D--WVTYKLEYSD-DGVNWT-TYKDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2208-2342 3.41e-30

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: 117.16  E-value: 3.41e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  2208 QITASSYFTNmfaTWSPSKArlhLQG-RSNAWRPQVNNPKEWLQVDFQKTMKVTGITTQGVKSlLTSMYVKEFLISSSQD 2286
Cdd:pfam00754    1 QITASSSYSG---EGPAAAA---LDGdPNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLD 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 426398029  2287 GHHWTLFFQNGkvkvFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWMHQ--IALRMEV 2342
Cdd:pfam00754   74 GENWTTVKDEK----IPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGngIALRAEL 127
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2055-2185 7.00e-28

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: 110.23  E-value: 7.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  2055 QITASGQYGQWAPKLARLHysGSIN-AWSTKE--PFSWIKVDLLAPMIIHGIKTQGaRQKFSSLYISQFIIMYSLDGKKW 2131
Cdd:pfam00754    1 QITASSSYSGEGPAAAALD--GDPNtAWSAWSgdDPQWIQVDLGKPKKITGVVTQG-RQDGSNGYVTSYKIEYSLDGENW 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 426398029  2132 QTYRGNSTgtlmvfFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRS--TLRMEL 2185
Cdd:pfam00754   78 TTVKDEKI------PGNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGNgiALRAEL 127
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 218-349 3.12e-15

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 75.05  E-value: 3.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   218 FAVFDEGKSWHsETKNSLMQDRDAASARAWPKM------HTVNGYVNRSLPGLIGCHRKSVYWHVIgMGTTPEVHSIFLE 291
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFppvpdaVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 426398029   292 GHTFLV--------RNHRQASLEISPITFLTAQTLLM-DLGQFLLFCH-ISSHQHDGMEAYVKVDSCP 349
Cdd:pfam00394   79 GHKMTVvevdgvyvNPFTVDSLDIFPGQRYSVLVTANqDPGNYWIVASpNIPAFDNGTAAAILRYSGA 146
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1915-2036 4.91e-10

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: 59.76  E-value: 4.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  1915 ERNCRAPCNIQMEDPTFkeNYRFHAINGYIMD-TLPGLVMAQDQRIRWYLLSMGSNenIHSIHFSGHVFTV-----RKKE 1988
Cdd:pfam07731    1 DTPPKLPTLLQITSGNF--RRNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTTG--VHPFHLHGHSFQVlgrggGPWP 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 426398029  1989 EYKMALYNL-----------YPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVY 2036
Cdd:pfam07731   77 EEDPKTYNLvdpvrrdtvqvPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVR 135
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 467-572 3.08e-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: 45.31  E-value: 3.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   467 ILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvrplysrRLPK-----GVKHLKDFPILPGEIFKYKWTVTVEDGpt 541
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL---------QQRGtpwmdGVPGVTQCPIPPGQSFTYRFQVKQQAG-- 92

                           90       100       110
                   ....*....|....*....|....*....|.
gi 426398029   542 ksdprclTRYYSSFINMERdlASGLIGPLLI 572
Cdd:pfam07732   93 -------TYWYHSHTSGQQ--AAGLAGAIII 114
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 90-197 2.74e-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: 42.62  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029    90 LLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVsywKASEGAEYD--DQTSQREKEddkvfPGGSHTYVWQVLKENGpma 167
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL---QQRGTPWMDgvPGVTQCPIP-----PGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 426398029   168 sdplclTYSYLSHVDLVKdlNSGLIGALLV 197
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 440-539 7.91e-04

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


Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 44.73  E-value: 7.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   440 RKYK-KVRFMAYTdETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSrrlpKGVKHLK 518
Cdd:TIGR03389    4 RHYTfDVQEKNVT-RLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQYNVTIHWHGVRQLRNGWA----DGPAYIT 78

                           90       100
                   ....*....|....*....|.
gi 426398029   519 DFPILPGEIFKYKWTVTVEDG 539
Cdd:TIGR03389   79 QCPIQPGQSYVYNFTITGQRG 99
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1903-2035 1.72e-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: 43.38  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1903 DETRSWYFTENMERNcrapcniqmedptfkenyrFHAINGYIMDTL-PGLVMAQDQRIRWYLLSMGSNenIHSIHFSGHV 1981
Cdd:COG2132   302 VRTRELVLTGGMAGY-------------------VWTINGKAFDPDrPDLTVKLGERERWTLVNDTMM--PHPFHLHGHQ 360

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029 1982 FTVRK---KEEYKMAL---YNLYPGvfETVEML---PSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:COG2132   361 FQVLSrngKPPPEGGWkdtVLVPPG--ETVRILfrfDNYPGDWMFHCHILEHEDAGMMGQFEV 421
 
Name Accession Description Interval E-value
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 399-575 5.04e-115

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: 361.94  E-value: 5.04e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  399 KTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGD 478
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  479 TLLIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINM 558
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 426398029  559 ERDLASGLIGPLLICYK 575
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-201 2.62e-110

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: 348.12  E-value: 2.62e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   22 RRYYLGAVELSWDYMQSDLGELPVDarfpprvPKSFPFNTSVVYKKTVFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYD 101
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGDPASE-------QRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  102 TVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHV 181
Cdd:cd14452    74 TVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQV 153

                         170       180
                  ....*....|....*....|
gi 426398029  182 DLVKDLNSGLIGALLVCREG 201
Cdd:cd14452   154 DPVKDVNSGLIGALLVCRMG 173
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1714-1880 1.17e-102

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: 326.07  E-value: 1.17e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1714 TRHYFIAAVERLWDYGMSSSPHVLR----NRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDN 1789
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPQHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1790 IMVTFKNQASRPYSFYSSLISYEEDQRqgAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSG 1869
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQR--AEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSG 158

                         170
                  ....*....|.
gi 426398029 1870 LIGPLLVCHTN 1880
Cdd:cd04228   159 LIGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1892-2035 1.54e-95

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: 304.50  E-value: 1.54e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1892 VQEFALFFTIFDETRSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNEN 1971
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 426398029 1972 IHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 401-575 6.33e-93

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: 298.55  E-value: 6.33e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  401 WVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTL 480
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAEVGDTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  481 LIIFKNQASRPYNIYPHGITDVRPLYSRRLP--KGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINM 558
Cdd:cd04199    81 KVHFKNKASRPYSIHPHGVSYEKDSEGASYSdqTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHVDL 160

                         170
                  ....*....|....*..
gi 426398029  559 ERDLASGLIGPLLICYK 575
Cdd:cd04199   161 EKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 22-200 3.94e-92

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: 296.24  E-value: 3.94e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   22 RRYYLGAVELSWDYMQSDLGELPVDARfpPRVPKSFPFNTSVVYKKTVFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYD 101
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKDLSYR--NQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAEVGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  102 TVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHV 181
Cdd:cd04199    79 TIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHV 158

                         170
                  ....*....|....*....
gi 426398029  182 DLVKDLNSGLIGALLVCRE 200
Cdd:cd04199   159 DLEKDINSGLIGPLLICKK 177
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 588-730 1.64e-88

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: 284.45  E-value: 1.64e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  588 DKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDF 667
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029  668 LSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSC 730
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 211-345 1.18e-80

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: 261.76  E-value: 1.18e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  211 LHKFILLFAVFDEGKSWHSETKNSLMQDRdAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIFL 290
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRDK-FKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 426398029  291 EGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKV 345
Cdd:cd11015    80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 1715-1879 2.46e-80

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: 262.34  E-value: 2.46e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1715 RHYFIAAVERLWDYGMSSSPHVLR-------NRAQSGSVPQFKKVVFQEFTDGSFTQPlyrGELNEHLGLLGPYIRAEVE 1787
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKDLsyrnqylDNGPFRIGRSYKKVVYREYTDESFTTP---GPQPEHLGILGPTIRAEVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1788 DNIMVTFKNQASRPYSFYSSLISYEEDQRQG--------AEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSD 1859
Cdd:cd04199    78 DTIKVHFKNKASRPYSIHPHGVSYEKDSEGAsysdqtgpDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSH 157

                         170       180
                  ....*....|....*....|
gi 426398029 1860 VDLEKDVHSGLIGPLLVCHT 1879
Cdd:cd04199   158 VDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 1892-2035 8.74e-69

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: 228.06  E-value: 8.74e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1892 VQEFALFFTIFDETRSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNEN 1971
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 426398029 1972 IHSIHFSGHVFTVRKkeeYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:cd04200    81 VHSIHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 588-727 1.22e-66

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: 221.90  E-value: 1.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  588 DKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSL-QLSVCLHEVAYWYILSIGAQTD 666
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLpGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 426398029  667 FLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKV 727
Cdd:cd04200    81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 399-573 1.68e-65

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: 220.13  E-value: 1.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  399 KTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQH--ESGILGPLLYGEV 476
Cdd:cd14450     1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRpkEEGILGPVIRAQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  477 GDTLLIIFKNQASRPYNIYPHGITdVRP-----LYSRRLPKGVKHLKdfPILPGEIFKYKWTVTVEDGPTKSDPRCLTRY 551
Cdd:cd14450    81 RDTIKIVFKNKASRPYSIYPHGVT-VSKaaegaSYPPDPRGNETQNK--AVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                         170       180
                  ....*....|....*....|..
gi 426398029  552 YSSFINMERDLASGLIGPLLIC 573
Cdd:cd14450   158 YHSAVDITRDIASGLIGPLLIC 179
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 211-345 4.43e-60

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 203.03  E-value: 4.43e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  211 LHKFILLFAVFDEGKSWHSETKNSLMQ------DRDAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPE 284
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCdnpekvDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 426398029  285 VHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKV 345
Cdd:cd04200    81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2195-2344 1.49e-58

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: 198.73  E-value: 1.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 2195 MPLGMESKAiSDAQITASSYFTnmfATWSPSKARLHlqgRSNAWRPQVNNPKEWLQVDFQKTMKVTGITTQGVKSLLTSM 2274
Cdd:cd00057     1 EPLGMESGL-ADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSE 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 2275 YVKEFLISSSQDGHHWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWMHQIALRMEVLG 2344
Cdd:cd00057    74 WVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-200 8.20e-58

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: 198.41  E-value: 8.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   22 RRYYLGAVELSWDYMQSD---LGELPVDARFPPRV-PKSFPFNTSVVYKKTVFVEFTDHLFNIAKPRPPWMGLLGPTIQA 97
Cdd:cd04222     1 REYYIGIRETQWDYAPSGknlITNQTFDDDEHASVfLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   98 EVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSY 177
Cdd:cd04222    81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 426398029  178 LSHVDLVKDLNSGLIGALLVCRE 200
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 22-201 7.04e-57

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: 194.69  E-value: 7.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   22 RRYYLGAVELSWDYmqsdlgelpvdaRFPPRVPKSFPFNTSvvYKKTVFVEFTDHlFNIAKPRPPWMGLLGPTIQAEVYD 101
Cdd:cd04226     1 REYYIAAQNIDWDY------------TPQSEELRLKRSEQS--FKKIVYREYEEG-FKKEKPADLSSGLLGPTLRAEVGD 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  102 TVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHV 181
Cdd:cd04226    66 TLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHV 145

                         170       180
                  ....*....|....*....|
gi 426398029  182 DLVKDLNSGLIGALLVCREG 201
Cdd:cd04226   146 NMVRDFNSGLIGALLICKKG 165
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1714-1877 7.58e-56

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: 192.36  E-value: 7.58e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1714 TRHYFIAAVERLWDY-GMSSSPHVLRNRAQSGsvpQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMV 1792
Cdd:cd14451     1 KRRYYIAAEEEEWDYaGYGKSRLDKTQNERDT---VFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1793 TFKNQASRPYSFYSSLISYE--------EDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEK 1864
Cdd:cd14451    78 FFKNLASRPYSLHAHGLSYEksseglsyDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEK 157

                         170
                  ....*....|...
gi 426398029 1865 DVHSGLIGPLLVC 1877
Cdd:cd14451   158 DIHSGLIGPLLIC 170
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2042-2187 1.95e-53

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: 184.09  E-value: 1.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 2042 TPLGMASGHiRDFQITASGQYG-QWAPKLARLHysgSINAWSTKE--PFSWIKVDLLAPMIIHGIKTQGARQKFSSLYIS 2118
Cdd:cd00057     1 EPLGMESGL-ADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVT 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 426398029 2119 QFIIMYSLDGKKWQTYRGNstGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMG 2187
Cdd:cd00057    77 SYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1712-1890 7.21e-52

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: 181.90  E-value: 7.21e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1712 KKTRHYFIAAVERLWDY---GMSSSPHVLRNRAQSGSVP-----------QFKKVVFQEFTDGSFTQPLYRGELNEHLGL 1777
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYapsGKNLFTGQNLTAPGSDSEVffqrnetriggTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1778 LGPYIRAEVEDNIMVTFKNQASRPYSFYSSLISYEEDQ-----RQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCK 1852
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYegamyRDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 426398029 1853 AWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNpAHGRQV 1890
Cdd:cd04224   161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLN-ANGRQK 197
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 21-201 9.25e-50

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: 174.64  E-value: 9.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   21 TRRYYLGAVELSWDYmqSDLGELPVDARFPPRvpksfpfntSVVYKKTVFVEFTDHLFNIAKPRPPW---MGLLGPTIQA 97
Cdd:cd14451     1 KRRYYIAAEEEEWDY--AGYGKSRLDKTQNER---------DTVFKKVVFRRYLDSTFSTPDIQGEYeehLGILGPVIRA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   98 EVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSY 177
Cdd:cd14451    70 EVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAY 149

                         170       180
                  ....*....|....*....|....
gi 426398029  178 LSHVDLVKDLNSGLIGALLVCREG 201
Cdd:cd14451   150 YSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 403-585 1.27e-49

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: 175.35  E-value: 1.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  403 HYIAAEEEDWDYAPL---------VLAPDDRSYKsqYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHES---GILGP 470
Cdd:cd04224     6 YFIAAEEIMWDYAPSgknlftgqnLTAPGSDSEV--FFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEehlGILGP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  471 LLYGEVGDTLLIIFKNQASRPYNIYPHGITDVR----PLYSRRLPKGVKHLKdfpilPGEIFKYKWTVTVEDGPTKSDPR 546
Cdd:cd04224    84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKnyegAMYRDGDPSPGSHVS-----PGETFTYEWTVPEGVGPTNQDPP 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 426398029  547 CLTRYYSSFINMERDLASGLIGPLLICYKESVDQRGNQI 585
Cdd:cd04224   159 CLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 402-575 1.34e-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: 171.83  E-value: 1.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  402 VHYIAAEEEDWDYAP--------LVLAPDDRSykSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLY 473
Cdd:cd04222     2 EYYIGIRETQWDYAPsgknlitnQTFDDDEHA--SVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  474 GEVGDTLLIIFKNQASRPYNIYPHGITDVR----PLYsrrlPKGVKHL--KDFPILPGEIFKYKWTVTVEDGPTKSDPRC 547
Cdd:cd04222    80 AEVGDVIVVHLKNFASRPYSLHPHGVFYNKenegALY----PDNTSGFekADDAVPPGGSYTYTWTVPEEQAPTKADANC 155

                         170       180
                  ....*....|....*....|....*...
gi 426398029  548 LTRYYSSFINMERDLASGLIGPLLICYK 575
Cdd:cd04222   156 LTRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-209 4.92e-45

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: 162.26  E-value: 4.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   22 RRYYLGAVELSWDYMQSDLGE---LPVDArfpprvPKS-----FPFNTSVV---YKKTVFVEFTDHLFNIAKPRPP---W 87
Cdd:cd04224     4 RHYFIAAEEIMWDYAPSGKNLftgQNLTA------PGSdsevfFQRNETRIggtYWKVRYVEYTDATFTTRKHRSKeeeH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   88 MGLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTsqrEKEDDKVFPGGSHTYVWQVLKENGPMA 167
Cdd:cd04224    78 LGILGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGD---PSPGSHVSPGETFTYEWTVPEGVGPTN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 426398029  168 SDPLCLTYSYLSHVDLVKDLNSGLIGALLVCREGSLAKEKTQ 209
Cdd:cd04224   155 QDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQ 196
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 403-575 4.95e-45

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: 161.10  E-value: 4.95e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  403 HYIAAEEEDWDYAPLVLAPDDR------SYKSQYLNNGPQRIGRKYKKVRFMAYTDETF---KTREAIQHESGILGPLLY 473
Cdd:cd04225     3 YYIAAEEVEWDYSPQRTWEQELhntheeSPGNAFLNKGDKFIGSKYKKVVYREYTDDTFsvpKERTAEEEHLGILGPLIH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  474 GEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSrrlpkgvkhlkdfPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYS 553
Cdd:cd04225    83 AEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVA-------------PTEPGETQTYTWKIPERSGPGVEDSNCISWAYY 149

                         170       180
                  ....*....|....*....|..
gi 426398029  554 SFINMERDLASGLIGPLLICYK 575
Cdd:cd04225   150 STVDQIKDLYSGLIGPLVICRR 171
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 588-721 3.40e-43

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: 155.03  E-value: 3.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  588 DKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQ-LSVCLHEVAYWYILSIGAQTD 666
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSApLGFCHSEVVQWHISSVGTQDE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 426398029  667 FLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGM 721
Cdd:cd14454    81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGL 135
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1892-2035 2.96e-42

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: 151.94  E-value: 2.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1892 VQEFALFFTIFDETRSWYFTENMERNCRapcNIQMEDPTFKENYRFHAINGYIMDtLPGLVMAQDQRIRWYLLSMGSNEN 1971
Cdd:cd14455     1 RREFVLLFMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 426398029 1972 IHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:cd14455    77 LHVVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 24-199 4.21e-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: 153.11  E-value: 4.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   24 YYLGAVELSWDYMQSdlgeLP--VDARFPPRVPKSFPFNTSVVYKKTVFVEFTDHLFN--IAKPRPPWMGLLGPTIQAEV 99
Cdd:cd14450     5 YFIAAEEVIWDYAPS----IPenMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTkrLENPRPKEEGILGPVIRAQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  100 YDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLS 179
Cdd:cd14450    81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHS 160

                         170       180
                  ....*....|....*....|
gi 426398029  180 HVDLVKDLNSGLIGALLVCR 199
Cdd:cd14450   161 AVDITRDIASGLIGPLLICK 180
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 403-575 1.70e-41

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: 150.78  E-value: 1.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  403 HYIAAEEEDWDYAPlvlapddrsyksQYLNNGPQRIGRKYKKVRFMAYtDETFKTREAIQHESGILGPLLYGEVGDTLLI 482
Cdd:cd04226     3 YYIAAQNIDWDYTP------------QSEELRLKRSEQSFKKIVYREY-EEGFKKEKPADLSSGLLGPTLRAEVGDTLIV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  483 IFKNQASRPYNIYPHGITDVR----PLYS-RRLPkgVKHLKDfPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFIN 557
Cdd:cd04226    70 HFKNMADKPLSIHPQGIAYGKksegSLYSdNTSP--VEKLDD-AVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVN 146

                         170
                  ....*....|....*...
gi 426398029  558 MERDLASGLIGPLLICYK 575
Cdd:cd04226   147 MVRDFNSGLIGALLICKK 164
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1715-1877 3.06e-40

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: 147.61  E-value: 3.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1715 RHYFIAAVERLWDYgmssSP--------HVLRNRAQS-----------GSvpQFKKVVFQEFTDGSFTQPLYRGELNEHL 1775
Cdd:cd04225     1 RTYYIAAEEVEWDY----SPqrtweqelHNTHEESPGnaflnkgdkfiGS--KYKKVVYREYTDDTFSVPKERTAEEEHL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1776 GLLGPYIRAEVEDNIMVTFKNQASRPYSFYSSLIsyeedqrQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWA 1855
Cdd:cd04225    75 GILGPLIHAEVGEKVKIVFKNMASRPYSIHAHGV-------KTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWA 147

                         170       180
                  ....*....|....*....|..
gi 426398029 1856 YFSDVDLEKDVHSGLIGPLLVC 1877
Cdd:cd04225   148 YYSTVDQIKDLYSGLIGPLVIC 169
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2039-2188 7.21e-40

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: 144.96  E-value: 7.21e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   2039 KCQTPLGMASghirDFQITASGQYgqWAPKLARLHYsGSINAWSTKEP--FSWIKVDLLAPMIIHGIKTQGArqkFSSLY 2116
Cdd:smart00231    1 PCNEPLGLES----DSQITASSSY--WAAKIARLNG-GSDGGWCPAKNdlPPWIQVDLGRLRTVTGVITGRR---HGNGD 70

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 426398029   2117 ISQFIIMYSLDGKKWQTYRGnstGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGC 2188
Cdd:smart00231   71 WVTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 588-730 1.27e-39

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: 144.55  E-value: 1.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  588 DKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQ-LSVCLHEVAYWYILSIGAQTD 666
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPgLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 426398029  667 FLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSC 730
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 588-727 1.32e-39

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: 144.54  E-value: 1.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  588 DKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSL-QLSVCLHEVAYWYILSIGAQTD 666
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLpGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 426398029  667 FLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKV 727
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1717-1877 3.99e-39

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: 144.63  E-value: 3.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1717 YFIAAVERLWDYGmSSSPHVLRNRAQSGSVPQF--------KKVVFQEFTDGSFTQPLYRGELNEhLGLLGPYIRAEVED 1788
Cdd:cd14450     5 YFIAAEEVIWDYA-PSIPENMDKRYRSQYLDNFsnnigkkyKKAVFTQYEDGSFTKRLENPRPKE-EGILGPVIRAQVRD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1789 NIMVTFKNQASRPYSFYS---SLISYEEDQRQGAEPRKNF-----VKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDV 1860
Cdd:cd14450    83 TIKIVFKNKASRPYSIYPhgvTVSKAAEGASYPPDPRGNEtqnkaVQPGETYTYKWNILETDEPTARDPRCLTRMYHSAV 162

                         170
                  ....*....|....*..
gi 426398029 1861 DLEKDVHSGLIGPLLVC 1877
Cdd:cd14450   163 DITRDIASGLIGPLLIC 179
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 403-575 5.29e-39

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: 143.83  E-value: 5.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  403 HYIAAEEEDWDYAPLVLAPDDRSYKSQylnngpqriGRKYKKVRFMAYTDETFKTREaIQHES----GILGPLLYGEVGD 478
Cdd:cd14451     4 YYIAAEEEEWDYAGYGKSRLDKTQNER---------DTVFKKVVFRRYLDSTFSTPD-IQGEYeehlGILGPVIRAEVDD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  479 TLLIIFKNQASRPYNIYPHGITDVRPL----YSRRLPKGVKhlKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSS 554
Cdd:cd14451    74 VIQVFFKNLASRPYSLHAHGLSYEKSSeglsYDDESPDWFK--KDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYS 151

                         170       180
                  ....*....|....*....|.
gi 426398029  555 FINMERDLASGLIGPLLICYK 575
Cdd:cd14451   152 AVNPEKDIHSGLIGPLLICRK 172
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1892-2035 6.14e-39

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: 142.70  E-value: 6.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1892 VQEFALFFTIFDETRSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNEN 1971
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 426398029 1972 IHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 22-201 2.21e-38

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: 142.17  E-value: 2.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   22 RRYYLGAVELSWDYMQS--DLGELPVDARFPPRVPKSFPFNTSVVYKKTVFVEFTDHLFNIAKPRPPWMGLLGPTIQAEV 99
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSgkNKCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  100 YDTVVITLKN-MASHPVSLHAVGVSYWKASEGAeyddqtsqREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYL 178
Cdd:cd04229    81 GDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGT--------TDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYH 152

                         170       180
                  ....*....|....*....|...
gi 426398029  179 SHVDLVKDLNSGLIGALLVCREG 201
Cdd:cd04229   153 SHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1893-2040 1.21e-37

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: 139.15  E-value: 1.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1893 QEFALFFTIFDETRSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENI 1972
Cdd:cd11022     2 KEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 426398029 1973 HSIHFSGHvfTVRKKEEYKMALyNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVysNKC 2040
Cdd:cd11022    82 HGIYFSGN--TFLLQGTRRDTA-NLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV--SQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1892-2035 1.44e-37

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: 138.76  E-value: 1.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1892 VQEFALFFTIFDETRSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNEN 1971
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 426398029 1972 IHSIHFSGHVFTVRKkeeYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:cd11021    81 IHSAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1715-1877 2.05e-37

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 139.34  E-value: 2.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1715 RHYFIAAVERLWDYGMSS--SPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELnehLGLLGPYIRAEVEDNIMV 1792
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDlgDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAW---MGLLGPTIVAEVGDTVVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1793 TFKNQASRPYSFYSSLISY--------EEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEK 1864
Cdd:cd14452    78 TFKNLASQPYSLHAVGVSYwkasegagYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVK 157

                         170
                  ....*....|...
gi 426398029 1865 DVHSGLIGPLLVC 1877
Cdd:cd14452   158 DVNSGLIGALLVC 170
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 402-572 2.57e-37

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: 139.09  E-value: 2.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  402 VHYIAAEEEDWDYAP----LVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVG 477
Cdd:cd04229     2 TYYIAAEEVDWDYAPsgknKCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRAEVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  478 DTLLIIFKNQASR-PYNIYPHGItdvrpLYSRRlPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFI 556
Cdd:cd04229    82 DTIKVVFKNNLDEfPVNMHPHGG-----LYSKD-NEGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHV 155

                         170
                  ....*....|....*.
gi 426398029  557 NMERDLASGLIGPLLI 572
Cdd:cd04229   156 DVFAHTNAGLVGPIIV 171
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1715-1877 2.14e-36

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: 136.78  E-value: 2.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1715 RHYFIAAVERLWDYGmSSSPHVLRNR-------AQS---------GSVpqFKKVVFQEFTDGSFTQPLyrgELNEHLGLL 1778
Cdd:cd04222     1 REYYIGIRETQWDYA-PSGKNLITNQtfdddehASVflkrgpdriGRV--YKKAVYLQYTDDTYRTEI---EKPVWLGFL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1779 GPYIRAEVEDNIMVTFKNQASRPYSFYSSLISYEE--------DQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFD 1850
Cdd:cd04222    75 GPILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKenegalypDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADAN 154

                         170       180
                  ....*....|....*....|....*..
gi 426398029 1851 CKAWAYFSDVDLEKDVHSGLIGPLLVC 1877
Cdd:cd04222   155 CLTRIYHSHIDAPKDIASGLIGPLIIC 181
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 403-573 7.12e-35

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 131.93  E-value: 7.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  403 HYIAAEEEDWDYAplvlapDDRSY---KSQYLNNGPQRIGRKYKKVRFMAYTDETFK---TREAIQHESGILGPLLYGEV 476
Cdd:cd04228     4 YFIAAVEVLWDYG------MQRPQhflRARDPNRGRRKSVPQYKKVVFREYLDGSFTqpvYRGELDEHLGILGPYIRAEV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  477 GDTLLIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKhlkdfpilPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFI 556
Cdd:cd04228    78 EDNIMVTFKNLASRPYSFHSSLISYEEDQRAEPRGNFVQ--------PGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNV 149

                         170
                  ....*....|....*..
gi 426398029  557 NMERDLASGLIGPLLIC 573
Cdd:cd04228   150 DLEKDLHSGLIGPLIIC 166
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 21-201 8.00e-35

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 131.93  E-value: 8.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   21 TRRYYLGAVELSWDYMQSDLGELpVDARFPPR-VPKSFPfntsvVYKKTVFVEFTDHLFNIAKPRPPW---MGLLGPTIQ 96
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPQHF-LRARDPNRgRRKSVP-----QYKKVVFREYLDGSFTQPVYRGELdehLGILGPYIR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   97 AEVYDTVVITLKNMASHPVSLHAVGVSYwkasegaeydDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYS 176
Cdd:cd04228    75 AEVEDNIMVTFKNLASRPYSFHSSLISY----------EEDQRAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWA 144

                         170       180
                  ....*....|....*....|....*
gi 426398029  177 YLSHVDLVKDLNSGLIGALLVCREG 201
Cdd:cd04228   145 YFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-199 1.90e-34

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: 131.05  E-value: 1.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   22 RRYYLGAVELSWDY---------MQSDLGELPVDarfpPRVPKSFPFNTSVvYKKTVFVEFTDHLFNIAKPRPPWM---G 89
Cdd:cd04225     1 RTYYIAAEEVEWDYspqrtweqeLHNTHEESPGN----AFLNKGDKFIGSK-YKKVVYREYTDDTFSVPKERTAEEehlG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   90 LLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVsywKASegaeyddqTSQREKeddkVFPGGSHTYVWQVLKENGPMASD 169
Cdd:cd04225    76 ILGPLIHAEVGEKVKIVFKNMASRPYSIHAHGV---KTD--------SSWVAP----TEPGETQTYTWKIPERSGPGVED 140

                         170       180       190
                  ....*....|....*....|....*....|
gi 426398029  170 PLCLTYSYLSHVDLVKDLNSGLIGALLVCR 199
Cdd:cd04225   141 SNCISWAYYSTVDQIKDLYSGLIGPLVICR 170
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2192-2345 4.11e-33

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: 125.70  E-value: 4.11e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   2192 SCSMPLGMESkaisDAQITASSyftnmfATWSPSKARLHlQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGITTQGVKSLL 2271
Cdd:smart00231    1 PCNEPLGLES----DSQITASS------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 426398029   2272 TsmYVKEFLISSSqDGHHWTlFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWMHQIALRMEVLGC 2345
Cdd:smart00231   70 D--WVTYKLEYSD-DGVNWT-TYKDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 403-573 1.89e-32

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: 125.09  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  403 HYIAAEEEDWDYAP---LVLAPDDRSYksqylnngPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDT 479
Cdd:cd14452     3 YYIAAVEIGWDYIHsdlGDPASEQRKK--------PKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGDT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  480 LLIIFKNQASRPYNIYPHGITDVRPL----YSRRLPKGVKhlKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSF 555
Cdd:cd14452    75 VVITFKNLASQPYSLHAVGVSYWKASegagYDDSTSQHEK--EDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQ 152

                         170
                  ....*....|....*...
gi 426398029  556 INMERDLASGLIGPLLIC 573
Cdd:cd14452   153 VDPVKDVNSGLIGALLVC 170
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 24-199 7.95e-32

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: 123.50  E-value: 7.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   24 YYLGAVELSWDYmqSDLGELPVDARFPPRVPKSFPFNTSVVYKKTVFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYDTV 103
Cdd:cd04227     5 HYIAAEELDWDY--APLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGDQI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  104 VITLKNMASHPVSLHAVGVSywkaSEGAEYDDQTSQREKE--DDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHV 181
Cdd:cd04227    83 HIMFKNTASRPYNIYPHGLT----SVRPMYRSRNPAGEKDlkTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTV 158

                         170
                  ....*....|....*...
gi 426398029  182 DLVKDLNSGLIGALLVCR 199
Cdd:cd04227   159 DPERDLASGLIGPLLICK 176
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 1715-1877 1.20e-31

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: 122.66  E-value: 1.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1715 RHYFIAAVERLWDYgmSSSPHVLRnraQSGSVPQFKKVVFQEFTDGsFTQPLYRGELNehlGLLGPYIRAEVEDNIMVTF 1794
Cdd:cd04226     1 REYYIAAQNIDWDY--TPQSEELR---LKRSEQSFKKIVYREYEEG-FKKEKPADLSS---GLLGPTLRAEVGDTLIVHF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1795 KNQASRPYSFYSSLISYEEdQRQGA---------EPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKD 1865
Cdd:cd04226    72 KNMADKPLSIHPQGIAYGK-KSEGSlysdntspvEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRD 150

                         170
                  ....*....|..
gi 426398029 1866 VHSGLIGPLLVC 1877
Cdd:cd04226   151 FNSGLIGALLIC 162
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1715-1876 1.85e-31

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: 122.53  E-value: 1.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1715 RHYFIAAVERLWDYGMS-------------SSPHVLRNRAQSGSVpqFKKVVFQEFTDGSFTQPLyrgELNEHLGLLGPY 1781
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSgknkcclgddlevSTLDSQPGPYTIGST--YTKARYREYTDNSFSTPK---PTPAYLGILGPV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1782 IRAEVEDNIMVTFKNQASR-PYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDV 1860
Cdd:cd04229    76 IRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHV 155

                         170
                  ....*....|....*.
gi 426398029 1861 DLEKDVHSGLIGPLLV 1876
Cdd:cd04229   156 DVFAHTNAGLVGPIIV 171
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1713-1877 2.74e-31

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: 121.96  E-value: 2.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1713 KTRHYFIAAVERLWDYgmssSPHV---LRNRAQSGSVP--------QFKKVVFQEFTDGSFTQplyRGELNEHLGLLGPY 1781
Cdd:cd04227     1 QTWEHYIAAEELDWDY----APLLsstDDRELQSRYLPtgpqrigyKYKKVAFVEYTDKTFKR---REAKQTEKGILGPL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1782 IRAEVEDNIMVTFKNQASRPYSFYSSLIS-----YEEDQRQGAEPRKNF-VKPNETKTYFWKVQHHMAPTKDEFDCKAWA 1855
Cdd:cd04227    74 LKGEVGDQIHIMFKNTASRPYNIYPHGLTsvrpmYRSRNPAGEKDLKTMpIGPGETFGYMWELTAEDGPTEEDPRCLTRL 153

                         170       180
                  ....*....|....*....|..
gi 426398029 1856 YFSDVDLEKDVHSGLIGPLLVC 1877
Cdd:cd04227   154 YQSTVDPERDLASGLIGPLLIC 175
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2208-2342 3.41e-30

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: 117.16  E-value: 3.41e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  2208 QITASSYFTNmfaTWSPSKArlhLQG-RSNAWRPQVNNPKEWLQVDFQKTMKVTGITTQGVKSlLTSMYVKEFLISSSQD 2286
Cdd:pfam00754    1 QITASSSYSG---EGPAAAA---LDGdPNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLD 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 426398029  2287 GHHWTLFFQNGkvkvFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWMHQ--IALRMEV 2342
Cdd:pfam00754   74 GENWTTVKDEK----IPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGngIALRAEL 127
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 589-727 9.03e-30

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: 116.51  E-value: 9.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  589 KRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQ-LSVCLHEVAYWYILSIGAQTDF 667
Cdd:cd11012     2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQgLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029  668 LSVFFSGYTF--KHKMVYE-DTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKV 727
Cdd:cd11012    82 HTAHFHGHSFdyKHRGVYRsDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 212-345 2.66e-28

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: 112.18  E-value: 2.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  212 HKFILLFAVFDEGKSWHSETK------NSLMQDRDAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEV 285
Cdd:cd11021     2 REFVLMFSVVDENLSWYLDENiktycsEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  286 HSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKV 345
Cdd:cd11021    82 HSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2055-2185 7.00e-28

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: 110.23  E-value: 7.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  2055 QITASGQYGQWAPKLARLHysGSIN-AWSTKE--PFSWIKVDLLAPMIIHGIKTQGaRQKFSSLYISQFIIMYSLDGKKW 2131
Cdd:pfam00754    1 QITASSSYSGEGPAAAALD--GDPNtAWSAWSgdDPQWIQVDLGKPKKITGVVTQG-RQDGSNGYVTSYKIEYSLDGENW 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 426398029  2132 QTYRGNSTgtlmvfFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRS--TLRMEL 2185
Cdd:pfam00754   78 TTVKDEKI------PGNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGNgiALRAEL 127
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 212-348 9.16e-27

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: 107.95  E-value: 9.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  212 HKFILLFAVFDEGKSWHSE------TKNSLMQDRDAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEV 285
Cdd:cd11022     2 KEFFLLFTVFDENESWYLDeniqqfTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029  286 HSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKVDSC 348
Cdd:cd11022    82 HGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1893-2035 4.80e-26

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: 105.37  E-value: 4.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1893 QEFALFFTIFDETRSWYfTENMERNCRApcniqmEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENI 1972
Cdd:cd11015     2 QAFVLLFAVFDEGKSWY-SEVGERKSRD------KFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029 1973 HSIHFSGHVFTVRKkeeYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:cd11015    75 HSIFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 593-727 2.08e-25

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 103.81  E-value: 2.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  593 ILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQ-LSVCLHEVAYWYILSIGAQTDFLSVF 671
Cdd:cd11018     6 LLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPgLVMAQHQRIRWHLLNMGSDEEIHSVH 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029  672 FSGYTF------KHKM-VYedtlTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKV 727
Cdd:cd11018    86 FHGLPFtvrakkEYRMgVY----NLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1897-2037 1.20e-23

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: 98.79  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1897 LFFTIFDETRSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPgLVMAQDQRIRWYLLSMGSNENIHSIH 1976
Cdd:cd11016     6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 426398029 1977 FSGHVFtvRKKEEYKMALyNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYS 2037
Cdd:cd11016    85 FSGNTF--KHQMVYEDVL-TLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVST 142
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1899-2015 6.29e-23

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: 96.86  E-value: 6.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1899 FTIFDETRSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFS 1978
Cdd:cd14454     8 FAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHLS 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 426398029 1979 GHVFTVRKKEEykmALYNLYPGVFETVEMLPSKAGIW 2015
Cdd:cd14454    88 GHTFRYKGKHE---DTLNLFPMSGESITVTMDNLGTW 121
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 212-345 6.55e-22

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 93.38  E-value: 6.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  212 HKFILLFAVFDEGKSWHSE--TKNSLMqdrdaasarawpkmHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIF 289
Cdd:cd14453     2 KEYVLMFGVFDENKSWYKQnaSVDSVK--------------YTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVH 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 426398029  290 LEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKV 345
Cdd:cd14453    68 FNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1893-2035 2.42e-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: 88.44  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1893 QEFALFFTIFDEtrswyftENMErncrapcniqmedptfkENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENI 1972
Cdd:cd11023     2 QEFIENSSIFLD-------LNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDF 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029 1973 HSIHFSGHvfTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:cd11023    58 HTPHWHGQ--TVEADKSRRTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 211-341 1.12e-19

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: 87.63  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  211 LHKFILLFAVFDEGKSWHSETK---------NSLMQDRDAasaRAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGT 281
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENmrrncrppcHIQTQDPWF---HINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029  282 TPEVHSIFLEGHTFLVR---NHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEA 341
Cdd:cd11018    78 DEEIHSVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSA 140
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 213-345 1.16e-17

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: 81.84  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  213 KFILLFAVFDEGKSWHSE------TKNSLMQDRDAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVH 286
Cdd:cd11012     3 EFALLFLVFDENESWYLDeniktySDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 426398029  287 SIFLEGHTFLVRN---HRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKV 345
Cdd:cd11012    83 TAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1893-2029 2.06e-17

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 80.29  E-value: 2.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1893 QEFALFFTIFDETRSWYftenmeRNCRAPCNIQmedptfkenyrfHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENI 1972
Cdd:cd14453     2 KEYVLMFGVFDENKSWY------KQNASVDSVK------------YTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 426398029 1973 HSIHFSGHVFtvrKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGM 2029
Cdd:cd14453    64 FSVHFNGQVL---EQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 215-339 1.14e-16

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: 79.15  E-value: 1.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  215 ILLFAVFDEGKSW-HSETKNSLMQDRDAASaRAWPK------MHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHS 287
Cdd:cd14454     5 HAVFAVFDENKSWyLEENINKYCSNPNNVK-KDDPKfyksniMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIIT 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 426398029  288 IFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGM 339
Cdd:cd14454    84 VHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGL 135
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 592-727 2.41e-16

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: 77.98  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  592 VILFSVFDENRSWYLTENIQRFLPNpagVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDFLSVF 671
Cdd:cd14455     5 VLLFMTFDEEKSWYYEKNRKRTCRE---NRVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVVH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 426398029  672 FSGYTFKHKMVYEDTLTLFPF---SGETVFMSMENPGLWILGCHNSDFRNRGMTALLKV 727
Cdd:cd14455    82 FHGQTFTEKGLKDHQLGVYPLlpgSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 218-349 3.12e-15

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 75.05  E-value: 3.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   218 FAVFDEGKSWHsETKNSLMQDRDAASARAWPKM------HTVNGYVNRSLPGLIGCHRKSVYWHVIgMGTTPEVHSIFLE 291
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFppvpdaVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 426398029   292 GHTFLV--------RNHRQASLEISPITFLTAQTLLM-DLGQFLLFCH-ISSHQHDGMEAYVKVDSCP 349
Cdd:pfam00394   79 GHKMTVvevdgvyvNPFTVDSLDIFPGQRYSVLVTANqDPGNYWIVASpNIPAFDNGTAAAILRYSGA 146
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 215-348 8.08e-15

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: 73.75  E-value: 8.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  215 ILLFAVFDEGKSW------HSETKNSLMQDRDAASARAWPKMHTVNGYVNRSLPGLIgCHRKSVYWHVIGMGTTPEVHSI 288
Cdd:cd11016     5 SLLFSVFDENNSWylkeniHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVI-CLTDVAYWYVLSVGAQTDFLSV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  289 FLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKVDSC 348
Cdd:cd11016    84 FFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 592-727 1.19e-14

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: 73.02  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  592 VILFSVFDENRSWYLTENiqrflpNPAGVQlEDPEFQASNIMHSINGYVFDSLQ-LSVCLHEVAYWYILSIGAQTDFLSV 670
Cdd:cd11015     5 VLLFAVFDEGKSWYSEVG------ERKSRD-KFKRADSRKEFHTINGYINASLPgLKICQRKPVIWHVIGMGTAPEVHSI 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 426398029  671 FFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKV 727
Cdd:cd11015    78 FFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 588-727 1.37e-14

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: 72.20  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  588 DKRNVILFSVFDENRSWYLTENiqrflpnpagvqledpefQASNIMHSINGYVFDSL-QLSVCLHEVAYWYILSIGAQTD 666
Cdd:cd14453     1 YKEYVLMFGVFDENKSWYKQNA------------------SVDSVKYTINGYTNGTLpDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 426398029  667 FLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKV 727
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 213-341 2.68e-14

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: 72.20  E-value: 2.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  213 KFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHT---VNGYVnRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIF 289
Cdd:cd14455     3 EFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPNVQDNHTfhaINGII-YNLKGLRMYTNELVRWHLINMGGPKDLHVVH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 426398029  290 LEGHTFL---VRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEA 341
Cdd:cd14455    82 FHGQTFTekgLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQT 136
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 250-339 3.29e-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: 68.02  E-value: 3.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  250 MHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASL-EISPITFLTAQTLLMDLGQFLLF 328
Cdd:cd11023    22 MHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRTDVaELMPASMRVADMTAADVGTWLLH 101

                          90
                  ....*....|.
gi 426398029  329 CHISSHQHDGM 339
Cdd:cd11023   102 CHVHDHYMAGM 112
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 624-727 4.62e-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: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  624 DPEFQASNIMHSINGYVFDSLQLSVCLH-EVAYWYILSIGAQTDFLSVFFSGYTFK-HKMVYEDTLTLFPFSGETVFMSM 701
Cdd:cd11023    13 DLNVEEAGLMHSINGYVFGNLPGVTIAKgKRVRWHLVAYGNEVDFHTPHWHGQTVEaDKSRRTDVAELMPASMRVADMTA 92

                          90       100
                  ....*....|....*....|....*.
gi 426398029  702 ENPGLWILGCHNSDFRNRGMTALLKV 727
Cdd:cd11023    93 ADVGTWLLHCHVHDHYMAGMMTQFAV 118
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1915-2036 4.91e-10

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: 59.76  E-value: 4.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  1915 ERNCRAPCNIQMEDPTFkeNYRFHAINGYIMD-TLPGLVMAQDQRIRWYLLSMGSNenIHSIHFSGHVFTV-----RKKE 1988
Cdd:pfam07731    1 DTPPKLPTLLQITSGNF--RRNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTTG--VHPFHLHGHSFQVlgrggGPWP 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 426398029  1989 EYKMALYNL-----------YPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVY 2036
Cdd:pfam07731   77 EEDPKTYNLvdpvrrdtvqvPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVR 135
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 89-198 7.24e-09

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: 55.75  E-value: 7.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   89 GLLGPTIQAEVYDTVVITLKN-MASHPVSLHAVGVSYWKASEGAEYDDQTSQRekeddkVFPGGSHTYVWQVlkengpma 167
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQCP------IPPGESFTYRFTV-------- 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 426398029  168 sDPLCLTYSYLSHVDLvkDLNSGLIGALLVC 198
Cdd:cd04206    93 -DDQAGTFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 466-573 1.89e-08

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: 54.60  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  466 GILGPLLYGEVGDTLLIIFKNQ-ASRPYNIYPHGItdvrplysrRLPK-----GVKHLKDFPILPGEIFKYKWTVtvedg 539
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGL---------RQPGtndgdGVAGLTQCPIPPGESFTYRFTV----- 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 426398029  540 ptksDPRCLTRYYSSFINMERdlASGLIGPLLIC 573
Cdd:cd04206    93 ----DDQAGTFWYHSHVGGQR--ADGLYGPLIVE 120
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1924-2033 1.22e-06

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: 49.77  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1924 IQMEDPTFKENYRFHAINGYIMDTLPG----LVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTV-RKKEEYKMALYNLY 1998
Cdd:cd04207     6 LVLSQTGAPDGTTRWVINGMPFKEGDAntdiFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFWVlGSGGGPFDAPLNLT 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 426398029 1999 PGVFETVEMLPS--------KA---GIWRVECLIGEHLHAGMSTLF 2033
Cdd:cd04207    86 NPPWRDTVLVPPggwvvirfKAdnpGVWMLHCHILEHEDAGMMTVF 131
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 469-572 5.42e-06

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


Pssm-ID: 259919 [Multi-domain]  Cd Length: 117  Bit Score: 47.68  E-value: 5.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  469 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSrrlpKGVKHLKDFPILPGEIFKYKWTVTVEDGptksdprcl 548
Cdd:cd13850    28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWS----DGVPGVTQWPIQPGGSFTYRWKAEDQYG--------- 94

                          90       100
                  ....*....|....*....|....
gi 426398029  549 TRYYSSFINMErdLASGLIGPLLI 572
Cdd:cd13850    95 LYWYHSHYRGY--YMDGLYGPIYI 116
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 466-572 6.22e-06

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: 47.23  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  466 GILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvrplysrRLPK---GVKHLKDFPILPGEIFKYKWTVtvedgPtk 542
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL---------RLPNamdGVPGLTQPPVPPGESFTYEFTP-----P-- 91

                          90       100       110
                  ....*....|....*....|....*....|
gi 426398029  543 sDPRclTRYYSSFINMERDLASGLIGPLLI 572
Cdd:cd13861    92 -DAG--TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 469-572 6.51e-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: 47.47  E-value: 6.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  469 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSrrlpKGVKHLKDFPILPGEIFKYKWtvtvedgptKSDPRCl 548
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKM----DGVPGVTQPAIEPGESFTYKF---------KAERPG- 96

                          90       100
                  ....*....|....*....|....*
gi 426398029  549 TRYYSSFINM-ERDLASGLIGPLLI 572
Cdd:cd13859    97 TLWYHCHVNVnEHVGMRGMWGPLIV 121
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 92-197 1.00e-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: 46.88  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   92 GPTIQAEVYDTVVITLKNMASHPVSLHAVGVsywkasegaeyddqtsQREKEDDKVF----PGGSHTYVWqVLKENGpma 167
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGI----------------HDAAMDGTGLgpimPGESFTYEF-VAEPAG--- 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 426398029  168 sdplclTYSYLSHVDLVKD-LNSGLIGALLV 197
Cdd:cd11024    92 ------THLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 469-572 1.08e-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: 46.87  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  469 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvrplYSRRLP--KGVKHLKDFPILPGEIFKYKWTVTVEDGptksdpr 546
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGL------FQNGTNwmDGTAGITQCPIPPGGSFTYNFTVDGQYG------- 96

                          90       100
                  ....*....|....*....|....*.
gi 426398029  547 clTRYYSSFINMErdLASGLIGPLLI 572
Cdd:cd13857    97 --TYWYHSHYSTQ--YADGLVGPLIV 118
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 92-197 1.61e-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: 46.10  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   92 GPTIQAEVYDTVVITLKNMASHPVSLHAVGVSywkaSEGAEYDDQT---SQREkeddkVFPGGSHTYVWQVLKENGpmas 168
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTagiTQCP-----IPPGGSFTYNFTVDGQYG---- 96

                          90       100
                  ....*....|....*....|....*....
gi 426398029  169 dplclTYSYLSHVDLvkDLNSGLIGALLV 197
Cdd:cd13857    97 -----TYWYHSHYST--QYADGLVGPLIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 467-572 3.08e-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: 45.31  E-value: 3.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   467 ILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvrplysrRLPK-----GVKHLKDFPILPGEIFKYKWTVTVEDGpt 541
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL---------QQRGtpwmdGVPGVTQCPIPPGQSFTYRFQVKQQAG-- 92

                           90       100       110
                   ....*....|....*....|....*....|.
gi 426398029   542 ksdprclTRYYSSFINMERdlASGLIGPLLI 572
Cdd:pfam07732   93 -------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 440-572 1.04e-04

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


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 43.97  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  440 RKYK-KVRFMAYTDETFKTReAIQHESGILGPLLYGEVGDTLLIIFKNQ-ASRPYNIYPHGITDV-RPLYSrrlpkGVKH 516
Cdd:cd13845     1 RHYKwKVEYMFWAPDCVEKL-VIGINGQFPGPTIRATAGDTIVVELENKlPTEGVAIHWHGIRQRgTPWAD-----GTAS 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 426398029  517 LKDFPILPGEIFKYKWTVtveDGPTksdprclTRYYSSFINMERdlASGLIGPLLI 572
Cdd:cd13845    75 VSQCPINPGETFTYQFVV---DRPG-------TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 89-197 1.21e-04

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 43.76  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   89 GLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQtsqrekedDKVFPGGSHTYVWQVlkengPMAS 168
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGLTQ--------PPVPPGESFTYEFTP-----PDAG 94

                          90       100
                  ....*....|....*....|....*....
gi 426398029  169 dplclTYSYLSHVDLVKDLNSGLIGALLV 197
Cdd:cd13861    95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 90-197 2.74e-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: 42.62  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029    90 LLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVsywKASEGAEYD--DQTSQREKEddkvfPGGSHTYVWQVLKENGpma 167
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL---QQRGTPWMDgvPGVTQCPIP-----PGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 426398029   168 sdplclTYSYLSHVDLVKdlNSGLIGALLV 197
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 456-572 4.44e-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: 41.88  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029  456 KTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGITdvrplysrrLP---KGVKHLKDFPILPGEIFKYKW 532
Cdd:cd13848    17 KEGEAITVNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLL---------LPndmDGVPGLSFPGIKPGETFTYRF 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 426398029  533 TVtVEDGptksdprclTRYYSSFINMERDlaSGLIGPLLI 572
Cdd:cd13848    88 PV-RQSG---------TYWYHSHSGLQEQ--TGLYGPIII 115
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 92-197 5.76e-04

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


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 41.66  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   92 GPTIQAEVYDTVVITLKN-MASHPVSLHAVGV----SYWkaSEGAEYDDQTSqrekeddkVFPGGSHTYVWQVLKENgpm 166
Cdd:cd13845    30 GPTIRATAGDTIVVELENkLPTEGVAIHWHGIrqrgTPW--ADGTASVSQCP--------INPGETFTYQFVVDRPG--- 96

                          90       100       110
                  ....*....|....*....|....*....|.
gi 426398029  167 asdplclTYSYLSHVDLVKdlNSGLIGALLV 197
Cdd:cd13845    97 -------TYFYHGHYGMQR--SAGLYGSLIV 118
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 440-539 7.91e-04

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


Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 44.73  E-value: 7.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   440 RKYK-KVRFMAYTdETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSrrlpKGVKHLK 518
Cdd:TIGR03389    4 RHYTfDVQEKNVT-RLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQYNVTIHWHGVRQLRNGWA----DGPAYIT 78

                           90       100
                   ....*....|....*....|.
gi 426398029   519 DFPILPGEIFKYKWTVTVEDG 539
Cdd:TIGR03389   79 QCPIQPGQSYVYNFTITGQRG 99
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 92-155 1.48e-03

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


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 40.71  E-value: 1.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 426398029   92 GPTIQAEVYDTVVITLKNMASHPVSLHAVGV----SYWkaSEGAEYDDQTSQRekeddkvfPGGSHTY 155
Cdd:cd13849    28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIrqlrSGW--ADGPAYITQCPIQ--------PGQSYTY 85
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1903-2035 1.72e-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: 43.38  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1903 DETRSWYFTENMERNcrapcniqmedptfkenyrFHAINGYIMDTL-PGLVMAQDQRIRWYLLSMGSNenIHSIHFSGHV 1981
Cdd:COG2132   302 VRTRELVLTGGMAGY-------------------VWTINGKAFDPDrPDLTVKLGERERWTLVNDTMM--PHPFHLHGHQ 360

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 426398029 1982 FTVRK---KEEYKMAL---YNLYPGvfETVEML---PSKAGIWRVECLIGEHLHAGMSTLFLV 2035
Cdd:COG2132   361 FQVLSrngKPPPEGGWkdtVLVPPG--ETVRILfrfDNYPGDWMFHCHILEHEDAGMMGQFEV 421
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 92-199 2.52e-03

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: 40.33  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029   92 GPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTsqrekeddkVFPGGSHTYVWQVLKENGPMASDPL 171
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNASI---------VAPGDTRIYTWRTHGGYRRADGSWA 99

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 426398029  172 CLTYSYLSHVDLV-------KDLNSGLIGALLVCR 199
Cdd:cd14449   100 EGTAGYWHYHDHVfgtehgtEGLSRGLYGALIVRR 134
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 1960-2035 2.83e-03

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 40.06  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 426398029 1960 RWYLLSMgSNE--NIHSIHFSGHVFTV----RKKEEYKM--ALYNLYPGvfETVE--MLPSKAGIWRVECLIGEHLHAGM 2029
Cdd:cd13906    55 RSYVLRL-VNEtaFLHPMHLHGHFFRVlsrnGRPVPEPFwrDTVLLGPK--ETVDiaFVADNPGDWMFHCHILEHQETGM 131


                  ....*.
gi 426398029 2030 STLFLV 2035
Cdd:cd13906   132 MGVIRV 137
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 469-535 2.90e-03

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: 39.56  E-value: 2.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426398029  469 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRplysrrlpkgVKHLKDFPILPGEIFKYKWTVT 535
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAA----------MDGTGLGPIMPGESFTYEFVAE 88
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1779-1847 5.03e-03

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: 39.18  E-value: 5.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 426398029 1779 GPYIRAEVEDNIMVTFKNQASRPYSFYSSLISYEEDQRQGAEPrknfVKPNETKTYFWKVQ-------H-HMAPTKD 1847
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGLGP----IMPGESFTYEFVAEpagthlyHcHVQPLKE 104
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 469-539 7.16e-03

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


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 38.39  E-value: 7.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 426398029  469 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSrrlpKGVKHLKDFPILPGEIFKYKWTVTVEDG 539
Cdd:cd13849    28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSGWA----DGPAYITQCPIQPGQSYTYRFTVTGQEG 94
 
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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