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Conserved domains on  [gi|569009649|ref|XP_006527855|]
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coagulation factor VIII isoform X3 [Mus musculus]

Protein Classification

CuRO_3_FVIII_like and FA58C domain-containing protein( domain architecture ID 10362929)

protein containing domains Cupredoxin, CuRO_3_FVIII_like, and FA58C

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 ...
 346-522 2.61e-105

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: 334.21  E-value: 2.61e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  346 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 425
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  426 TLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 505
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 569009649  506 ERDLASGLIGPLLICYK 522
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1631-1795 3.23e-94

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


The actual alignment was detected with superfamily member cd04228:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 169  Bit Score: 301.81  E-value: 3.23e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1631 TRHYFIAAVERLWDYGMSTS-HVLR----NRYQSDNVPQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDN 1705
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPqHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1706 IMVTFKNQASRPYSFYSSLISYKEDQRGeEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMHSGL 1785
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQRA-EPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGL 159

                         170
                  ....*....|
gi 569009649 1786 IGPLLICHAN 1795
Cdd:cd04228   160 IGPLIICKTG 169
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1807-1950 1.67e-88

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


The actual alignment was detected with superfamily member cd11018:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 144  Bit Score: 284.47  E-value: 1.67e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1807 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1886
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009649 1887 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1950
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 4-149 6.86e-87

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


The actual alignment was detected with superfamily member cd14452:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 173  Bit Score: 281.10  E-value: 6.86e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649    4 SFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYED 83
Cdd:cd14452    28 KKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDD 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009649   84 QTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCKEG 149
Cdd:cd14452   108 STSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVKDVNSGLIGALLVCRMG 173
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 535-677 2.85e-80

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


The actual alignment was detected with superfamily member cd11016:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 143  Bit Score: 260.96  E-value: 2.85e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  535 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDF 614
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009649  615 LSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 677
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 159-293 1.88e-72

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


The actual alignment was detected with superfamily member cd11015:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 134  Bit Score: 238.27  E-value: 1.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  159 LYQFVLLFAVFDEGKSWHSETNDSYTQSmDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 238
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRD-KFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009649  239 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 293
Cdd:cd11015    80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2111-2259 3.54e-54

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: 186.02  E-value: 3.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 2111 PLGMESKvISDTQITASSYFTnmfATWSPSQARLHlqgRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSLFTSMF 2190
Cdd:cd00057     2 PLGMESG-LADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009649 2191 VKEFLISSSQDGHHWTQILYNGKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILG 2259
Cdd:cd00057    75 VTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1958-2102 1.29e-49

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: 173.31  E-value: 1.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1958 PLGMASGsIRDFQITASGHYG-QWAPNLARLHysgSINAWSTKE--PFSWIKVDLLAPMIVHGIKTQGARQKFSSLYISQ 2034
Cdd:cd00057     2 PLGMESG-LADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009649 2035 FIIMYSLDGKKWLSYQGNstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMG 2102
Cdd:cd00057    78 YKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
rpoC2 super family cl33332
RNA polymerase beta'' subunit; Reviewed
 1081-1456 2.57e-05

RNA polymerase beta'' subunit; Reviewed


The actual alignment was detected with superfamily member CHL00117:

Pssm-ID: 214368 [Multi-domain]  Cd Length: 1364  Bit Score: 49.94  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1081 NGNNSLNSEQEHSPKQLVYLMFKKYVKNQSFLSEKNKVTVEqdgFTKNIGLKdmafphnmSIFLTTLSNVHENGRHNQEK 1160
Cdd:CHL00117  741 PGTGKKNSKESKKIKNWIYVQRITPTKKKYFVLVRPVVTYE---IADGINLA--------TLFPQDLLQEKDNLQLRVVN 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1161 NIQEEIEKEalIEEkvvlpqvheaTGSKNFLKDILILGTRQ---NISLYEVH---VPVLQNitsiNNSTNTVQIHM--EH 1232
Cdd:CHL00117  810 YILYGNGKP--IRG----------ISSIQLVRTCLVLNWDQdkkSSSIEEARasfVEVRTN----GLIRDFLRINLvkSP 873

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1233 FFKRRKDKETNSEGLVNKTremvKNYPSQKNIttqrskraLGQFRLSTQWLKTincsTQCIIKQI-DHSKEMKKFITKSS 1311
Cdd:CHL00117  874 ISYIRKRNDPSSSGLLVQS----NNFLDSTNI--------YSKAEIQSQSLSQ----NQGTIRTLlNRNKESQSLLILSS 937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1312 lSDSSVIKSTTQTNSSDSHIVKTSAFPPIDLKRSPFQNKFSHVQASSYIYDFKTKSSRIqesNNFLKETKINNPSLAILP 1391
Cdd:CHL00117  938 -SDCFRIGPFNGKKSKYHNIKESNPLIPIRNSLGPLGTVLQIANFSSSYHLLTHNQILV---TKYLQLDNLKQTFQVKVL 1013

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009649 1392 WNMFIDQ-GKFTSPgKSNTNSVTYKKRENIIFLKPTLPEESGKIELLPQvSIQEEEILPTETSHGS 1456
Cdd:CHL00117 1014 KYYLIDEnGKIYNP-DPCSNIILNPFNLNWYFLHHNYCEETSTIISLGQ-FICENVCISKNGPHKS 1077
 
Name Accession Description Interval E-value
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 346-522 2.61e-105

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: 334.21  E-value: 2.61e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  346 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 425
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  426 TLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 505
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 569009649  506 ERDLASGLIGPLLICYK 522
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1631-1795 3.23e-94

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: 301.81  E-value: 3.23e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1631 TRHYFIAAVERLWDYGMSTS-HVLR----NRYQSDNVPQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDN 1705
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPqHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1706 IMVTFKNQASRPYSFYSSLISYKEDQRGeEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMHSGL 1785
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQRA-EPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGL 159

                         170
                  ....*....|
gi 569009649 1786 IGPLLICHAN 1795
Cdd:cd04228   160 IGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1807-1950 1.67e-88

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: 284.47  E-value: 1.67e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1807 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1886
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009649 1887 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1950
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 4-149 6.86e-87

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: 281.10  E-value: 6.86e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649    4 SFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYED 83
Cdd:cd14452    28 KKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDD 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009649   84 QTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCKEG 149
Cdd:cd14452   108 STSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 535-677 2.85e-80

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: 260.96  E-value: 2.85e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  535 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDF 614
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009649  615 LSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 677
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 159-293 1.88e-72

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: 238.27  E-value: 1.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  159 LYQFVLLFAVFDEGKSWHSETNDSYTQSmDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 238
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRD-KFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009649  239 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 293
Cdd:cd11015    80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2111-2259 3.54e-54

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: 186.02  E-value: 3.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 2111 PLGMESKvISDTQITASSYFTnmfATWSPSQARLHlqgRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSLFTSMF 2190
Cdd:cd00057     2 PLGMESG-LADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009649 2191 VKEFLISSSQDGHHWTQILYNGKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILG 2259
Cdd:cd00057    75 VTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1958-2102 1.29e-49

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: 173.31  E-value: 1.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1958 PLGMASGsIRDFQITASGHYG-QWAPNLARLHysgSINAWSTKE--PFSWIKVDLLAPMIVHGIKTQGARQKFSSLYISQ 2034
Cdd:cd00057     2 PLGMESG-LADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009649 2035 FIIMYSLDGKKWLSYQGNstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMG 2102
Cdd:cd00057    78 YKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1955-2103 4.27e-38

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: 139.95  E-value: 4.27e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   1955 CQIPLGMASgsirDFQITASGHYgqWAPNLARLHYsGSINAWSTKEP--FSWIKVDLLAPMIVHGIKTQGArqkFSSLYI 2032
Cdd:smart00231    2 CNEPLGLES----DSQITASSSY--WAAKIARLNG-GSDGGWCPAKNdlPPWIQVDLGRLRTVTGVITGRR---HGNGDW 71

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009649   2033 SQFIIMYSLDGKKWLSYQGnstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMGC 2103
Cdd:smart00231   72 VTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2107-2260 1.89e-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: 126.86  E-value: 1.89e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   2107 SCSIPLGMESkvisDTQITASSyftnmfATWSPSQARLHlQGRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlf 2186
Cdd:smart00231    1 PCNEPLGLES----DSQITASS------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHG-- 67

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009649   2187 TSMFVKEFLISSSqDGHHWTqILYNGKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILGC 2260
Cdd:smart00231   68 NGDWVTYKLEYSD-DGVNWT-TYKDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2123-2257 1.42e-29

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: 115.24  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  2123 QITASSYFTNmfaTWsPSQARLHLQGRTnAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlFTSMFVKEFLISSSQDG 2202
Cdd:pfam00754    1 QITASSSYSG---EG-PAAAALDGDPNT-AWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009649  2203 HHWTQIlyngKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIW--EHQIALRLEI 2257
Cdd:pfam00754   75 ENWTTV----KDEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWngGNGIALRAEL 127
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1970-2100 3.02e-26

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


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 105.61  E-value: 3.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  1970 QITASGHY-GQWAPNlARLHysGSIN-AWSTKE--PFSWIKVDLLAPMIVHGIKTQGaRQKFSSLYISQFIIMYSLDGKK 2045
Cdd:pfam00754    1 QITASSSYsGEGPAA-AALD--GDPNtAWSAWSgdDPQWIQVDLGKPKKITGVVTQG-RQDGSNGYVTSYKIEYSLDGEN 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009649  2046 WLSYQGNSTgtlmvfFGNVDSSGIKHNSFNPPIIARYIRLHPT--HSSIRSTLRMEL 2100
Cdd:pfam00754   77 WTTVKDEKI------PGNNDNNTPVTNTFDPPIKARYVRIVPTswNGGNGIALRAEL 127
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 166-297 1.65e-12

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: 66.96  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   166 FAVFDEGKSWHSETNDSYTQSMDsASARDWPKM------HTVNGYVNRSLPGLIGCHRKSVYWHVIgMGTTPEIHSIFLE 239
Cdd:pfam00394    1 EDYVITLSDWYHKDAKDLEKELL-ASGKAPTDFppvpdaVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009649   240 GHTF--------FVRNHRQASLEISPITFLTAQ-TLLIDLGQFLLFCH-ISSHKHDGMEAYVKVDSCP 297
Cdd:pfam00394   79 GHKMtvvevdgvYVNPFTVDSLDIFPGQRYSVLvTANQDPGNYWIVASpNIPAFDNGTAAAILRYSGA 146
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1831-1954 2.18e-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: 60.53  E-value: 2.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  1831 RNCKTPCNFQMEDPTLkeNYRFHAINGYVMD-TLPGLVMAQDQRIRWYLLsmgNNENI-QSIHFSGHVFTV-----RKKE 1903
Cdd:pfam07731    2 TPPKLPTLLQITSGNF--RRNDWAINGLLFPpNTNVITLPYGTVVEWVLQ---NTTTGvHPFHLHGHSFQVlgrggGPWP 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009649  1904 EYKMAVYNL-----------YPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVYSKQ 1954
Cdd:pfam07731   77 EEDPKTYNLvdpvrrdtvqvPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
rpoC2 CHL00117
RNA polymerase beta'' subunit; Reviewed
 1081-1456 2.57e-05

RNA polymerase beta'' subunit; Reviewed


Pssm-ID: 214368 [Multi-domain]  Cd Length: 1364  Bit Score: 49.94  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1081 NGNNSLNSEQEHSPKQLVYLMFKKYVKNQSFLSEKNKVTVEqdgFTKNIGLKdmafphnmSIFLTTLSNVHENGRHNQEK 1160
Cdd:CHL00117  741 PGTGKKNSKESKKIKNWIYVQRITPTKKKYFVLVRPVVTYE---IADGINLA--------TLFPQDLLQEKDNLQLRVVN 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1161 NIQEEIEKEalIEEkvvlpqvheaTGSKNFLKDILILGTRQ---NISLYEVH---VPVLQNitsiNNSTNTVQIHM--EH 1232
Cdd:CHL00117  810 YILYGNGKP--IRG----------ISSIQLVRTCLVLNWDQdkkSSSIEEARasfVEVRTN----GLIRDFLRINLvkSP 873

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1233 FFKRRKDKETNSEGLVNKTremvKNYPSQKNIttqrskraLGQFRLSTQWLKTincsTQCIIKQI-DHSKEMKKFITKSS 1311
Cdd:CHL00117  874 ISYIRKRNDPSSSGLLVQS----NNFLDSTNI--------YSKAEIQSQSLSQ----NQGTIRTLlNRNKESQSLLILSS 937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1312 lSDSSVIKSTTQTNSSDSHIVKTSAFPPIDLKRSPFQNKFSHVQASSYIYDFKTKSSRIqesNNFLKETKINNPSLAILP 1391
Cdd:CHL00117  938 -SDCFRIGPFNGKKSKYHNIKESNPLIPIRNSLGPLGTVLQIANFSSSYHLLTHNQILV---TKYLQLDNLKQTFQVKVL 1013

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009649 1392 WNMFIDQ-GKFTSPgKSNTNSVTYKKRENIIFLKPTLPEESGKIELLPQvSIQEEEILPTETSHGS 1456
Cdd:CHL00117 1014 KYYLIDEnGKIYNP-DPCSNIILNPFNLNWYFLHHNYCEETSTIISLGQ-FICENVCISKNGPHKS 1077
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 387-486 8.94e-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: 44.34  E-value: 8.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   387 RKYK-KVRFIAYTdETFKTRETIQHESGLLGPLLYGEVGDTLLIIFKNQASrpYNIYPHgitdvspLHARRLPR-----G 460
Cdd:TIGR03389    4 RHYTfDVQEKNVT-RLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQ--YNVTIH-------WHGVRQLRngwadG 73

                           90       100
                   ....*....|....*....|....*.
gi 569009649   461 IKHVKDLPIHPGEIFKYKWTVTVEDG 486
Cdd:TIGR03389   74 PAYITQCPIQPGQSYVYNFTITGQRG 99
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 414-519 2.58e-03

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 39.92  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   414 LLGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksd 491
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL------QQRGTPwmDGVPGVTQCPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 569009649   492 prclTRYYSSFINPERdlASGLIGPLLI 519
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
 
Name Accession Description Interval E-value
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 346-522 2.61e-105

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: 334.21  E-value: 2.61e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  346 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 425
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  426 TLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 505
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 569009649  506 ERDLASGLIGPLLICYK 522
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1631-1795 3.23e-94

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: 301.81  E-value: 3.23e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1631 TRHYFIAAVERLWDYGMSTS-HVLR----NRYQSDNVPQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDN 1705
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPqHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1706 IMVTFKNQASRPYSFYSSLISYKEDQRGeEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMHSGL 1785
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQRA-EPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGL 159

                         170
                  ....*....|
gi 569009649 1786 IGPLLICHAN 1795
Cdd:cd04228   160 IGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1807-1950 1.67e-88

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: 284.47  E-value: 1.67e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1807 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1886
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009649 1887 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1950
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 4-149 6.86e-87

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: 281.10  E-value: 6.86e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649    4 SFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYED 83
Cdd:cd14452    28 KKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDD 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009649   84 QTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCKEG 149
Cdd:cd14452   108 STSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 348-522 1.03e-82

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: 269.28  E-value: 1.03e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  348 WIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGDTL 427
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAEVGDTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  428 LIIFKNQASRPYNIYPHGITDVSPLHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 505
Cdd:cd04199    81 KVHFKNKASRPYSIHPHGVSYEKDSEGASYSdqTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHVDL 160

                         170
                  ....*....|....*..
gi 569009649  506 ERDLASGLIGPLLICYK 522
Cdd:cd04199   161 EKDINSGLIGPLLICKK 177
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 535-677 2.85e-80

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: 260.96  E-value: 2.85e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  535 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDF 614
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009649  615 LSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 677
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 4-148 1.92e-74

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: 245.78  E-value: 1.92e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649    4 SFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYED 83
Cdd:cd04199    33 NGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSD 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569009649   84 QTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCKE 148
Cdd:cd04199   113 QTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 159-293 1.88e-72

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: 238.27  E-value: 1.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  159 LYQFVLLFAVFDEGKSWHSETNDSYTQSmDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 238
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRD-KFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009649  239 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 293
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 ...
 1632-1794 2.25e-72

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: 239.61  E-value: 2.25e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1632 RHYFIAAVERLWDYGMSTSH--------VLRNRYQSDNVPQFKKVVFQEFTDGSFSQPlyrGELNEHLGLLGPYIRAEVE 1703
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAekdlsyrnQYLDNGPFRIGRSYKKVVYREYTDESFTTP---GPQPEHLGILGPTIRAEVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1704 DNIMVTFKNQASRPYSFYSSLISYKEDQRG---------EEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSD 1774
Cdd:cd04199    78 DTIKVHFKNKASRPYSIHPHGVSYEKDSEGasysdqtgpDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSH 157

                         170       180
                  ....*....|....*....|
gi 569009649 1775 VDLERDMHSGLIGPLLICHA 1794
Cdd:cd04199   158 VDLEKDINSGLIGPLLICKK 177
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 346-520 5.68e-64

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: 215.90  E-value: 5.68e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  346 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQH--ESGLLGPLLYGEV 423
Cdd:cd14450     1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRpkEEGILGPVIRAQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  424 GDTLLIIFKNQASRPYNIYPHGITdVSP-----LHARRLPRGIKHVKdlPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRY 498
Cdd:cd14450    81 RDTIKIVFKNKASRPYSIYPHGVT-VSKaaegaSYPPDPRGNETQNK--AVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                         170       180
                  ....*....|....*....|..
gi 569009649  499 YSSFINPERDLASGLIGPLLIC 520
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 ...
 1807-1950 3.25e-63

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 211.88  E-value: 3.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1807 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1886
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009649 1887 IQSIHFSGHVFTVRKkeeYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1950
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 ...
 535-674 3.01e-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: 203.41  E-value: 3.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  535 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTD 613
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPgLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009649  614 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 674
Cdd:cd04200    81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 13-149 4.18e-56

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


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 192.77  E-value: 4.18e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   13 YKKTVFVEYKDQlFNIAKPRPPWMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKED 92
Cdd:cd04226    30 FKKIVYREYEEG-FKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLD 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009649   93 DKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCKEG 149
Cdd:cd04226   109 DAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1631-1792 3.03e-55

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 190.44  E-value: 3.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1631 TRHYFIAAVERLWDY-GMSTSHVLRNRYQSDNVpqFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDNIMVT 1709
Cdd:cd14451     1 KRRYYIAAEEEEWDYaGYGKSRLDKTQNERDTV--FKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1710 FKNQASRPYSFYSSLISYKEDQRG-----EEP----RRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERD 1780
Cdd:cd14451    79 FKNLASRPYSLHAHGLSYEKSSEGlsyddESPdwfkKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKD 158

                         170
                  ....*....|..
gi 569009649 1781 MHSGLIGPLLIC 1792
Cdd:cd14451   159 IHSGLIGPLLIC 170
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 161-293 9.49e-55

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: 187.62  E-value: 9.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  161 QFVLLFAVFDEGKSWHSETNDSYTQS------MDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 234
Cdd:cd04200     3 EFVLLFAVFDENKSWYLEDNIKRFCDnpekvdKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569009649  235 SIFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 293
Cdd:cd04200    83 SIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2111-2259 3.54e-54

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: 186.02  E-value: 3.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 2111 PLGMESKvISDTQITASSYFTnmfATWSPSQARLHlqgRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSLFTSMF 2190
Cdd:cd00057     2 PLGMESG-LADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009649 2191 VKEFLISSSQDGHHWTQILYNGKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILG 2259
Cdd:cd00057    75 VTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 13-148 8.86e-52

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: 181.08  E-value: 8.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   13 YKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKED 92
Cdd:cd04222    48 YKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKAD 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569009649   93 DKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCKE 148
Cdd:cd04222   128 DAVPPGGSYTYTWTVPEEQAPTKADANCLTRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 350-531 3.22e-50

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: 176.89  E-value: 3.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  350 HYISAEEEDWDYAPS-------VPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHES---GLLGPLL 419
Cdd:cd04224     6 YFIAAEEIMWDYAPSgknlftgQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEehlGILGPVI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  420 YGEVGDTLLIIFKNQASRPYNIYPHGI-----TDVSPLHARRLPRGikhvkdLPIHPGEIFKYKWTVTVEDGPTKSDPRC 494
Cdd:cd04224    86 RAEVGDTIKVTFRNKASRPFSIQPHGVfyeknYEGAMYRDGDPSPG------SHVSPGETFTYEWTVPEGVGPTNQDPPC 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 569009649  495 LTRYYSSFINPERDLASGLIGPLLICYKESVDQRGNQ 531
Cdd:cd04224   160 LTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQ 196
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1958-2102 1.29e-49

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: 173.31  E-value: 1.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1958 PLGMASGsIRDFQITASGHYG-QWAPNLARLHysgSINAWSTKE--PFSWIKVDLLAPMIVHGIKTQGARQKFSSLYISQ 2034
Cdd:cd00057     2 PLGMESG-LADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009649 2035 FIIMYSLDGKKWLSYQGNstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMG 2102
Cdd:cd00057    78 YKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1630-1805 7.45e-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: 173.04  E-value: 7.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1630 KTRHYFIAAVERLWDYGMS----TSHVLRNRYQSDNVP-----------QFKKVVFQEFTDGSFSQPLYRGELNEHLGLL 1694
Cdd:cd04224     2 KVRHYFIAAEEIMWDYAPSgknlFTGQNLTAPGSDSEVffqrnetriggTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1695 GPYIRAEVEDNIMVTFKNQASRPYSFYSSLISYKEDQRGEEPRRNF------VKPNETKIYFWKVQHHMAPTEDEFDCKA 1768
Cdd:cd04224    82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDpspgshVSPGETFTYEWTVPEGVGPTNQDPPCLT 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 569009649 1769 WAYFSDVDLERDMHSGLIGPLLICHANTLNpAHGRQV 1805
Cdd:cd04224   162 YLYFSAVDPVRDTNSGLVGPLLVCKKGSLN-ANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 349-522 1.39e-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: 1.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  349 IHYISAEEEDWDYAPSV------PTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFktRETIQHES--GLLGPLLY 420
Cdd:cd04222     2 EYYIGIRETQWDYAPSGknlitnQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTY--RTEIEKPVwlGFLGPILK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  421 GEVGDTLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHV--KDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRY 498
Cdd:cd04222    80 AEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFekADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRI 159

                         170       180
                  ....*....|....*....|....
gi 569009649  499 YSSFINPERDLASGLIGPLLICYK 522
Cdd:cd04222   160 YHSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 349-522 8.11e-44

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 157.63  E-value: 8.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  349 IHYISAEEEDWDYAPSVPTSD------NGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETF---KTRETIQHESGLLGPLL 419
Cdd:cd04225     2 TYYIAAEEVEWDYSPQRTWEQelhnthEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFsvpKERTAEEEHLGILGPLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  420 YGEVGDTLLIIFKNQASRPYNIYPHGITDVSPLHArrlprgikhvkdlPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYY 499
Cdd:cd04225    82 HAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVA-------------PTEPGETQTYTWKIPERSGPGVEDSNCISWAY 148

                         170       180
                  ....*....|....*....|...
gi 569009649  500 SSFINPERDLASGLIGPLLICYK 522
Cdd:cd04225   149 YSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 13-157 4.40e-43

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: 156.48  E-value: 4.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   13 YKKTVFVEYKDQLFNIAKPRPP---WMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTsqmE 89
Cdd:cd04224    52 YWKVRYVEYTDATFTTRKHRSKeeeHLGILGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGD---P 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009649   90 KEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCKEGSLSKERTQ 157
Cdd:cd04224   129 SPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQ 196
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1-149 4.62e-42

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: 152.69  E-value: 4.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649    1 MSTSFPFNTSimYKKTVFVEYKDQLFNIAKPRPPW---MGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASE 77
Cdd:cd14451    24 DKTQNERDTV--FKKVVFRRYLDSTFSTPDIQGEYeehLGILGPVIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSE 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009649   78 GDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCKEG 149
Cdd:cd14451   102 GLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1634-1792 3.70e-40

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: 147.72  E-value: 3.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1634 YFIAAVERLWDYGMSTSHVLRNRYQS---DNVPQF-----KKVVFQEFTDGSFSQPLYRGELNEhLGLLGPYIRAEVEDN 1705
Cdd:cd14450     5 YFIAAEEVIWDYAPSIPENMDKRYRSqylDNFSNNigkkyKKAVFTQYEDGSFTKRLENPRPKE-EGILGPVIRAQVRDT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1706 IMVTFKNQASRPYSFYSSLISYKEDQRG----EEPRRNF-----VKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVD 1776
Cdd:cd14450    84 IKIVFKNKASRPYSIYPHGVTVSKAAEGasypPDPRGNEtqnkaVQPGETYTYKWNILETDEPTARDPRCLTRMYHSAVD 163

                         170
                  ....*....|....*.
gi 569009649 1777 LERDMHSGLIGPLLIC 1792
Cdd:cd14450   164 ITRDIASGLIGPLLIC 179
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1632-1792 4.77e-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: 146.84  E-value: 4.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1632 RHYFIAAVERLWDYGMSTS-----HVLRNRYQSDNV---------PQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPY 1697
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTweqelHNTHEESPGNAFlnkgdkfigSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1698 IRAEVEDNIMVTFKNQASRPYSFYSSLIsyKEDQrgeePRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDL 1777
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGV--KTDS----SWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQ 154

                         170
                  ....*....|....*
gi 569009649 1778 ERDMHSGLIGPLLIC 1792
Cdd:cd04225   155 IKDLYSGLIGPLVIC 169
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1807-1950 5.23e-40

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: 145.39  E-value: 5.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1807 VQEFALLFTIFDETKSWYFTENVKRNCKtpcNFQMEDPTLKENYRFHAINGYVMDtLPGLVMAQDQRIRWYLLSMGNNEN 1886
Cdd:cd14455     1 RREFVLLFMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009649 1887 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1950
Cdd:cd14455    77 LHVVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 535-668 8.66e-39

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: 142.32  E-value: 8.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  535 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTD 613
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSApLGFCHSEVVQWHISSVGTQDE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009649  614 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGM 668
Cdd:cd14454    81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGL 135
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1807-1950 1.29e-38

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 141.93  E-value: 1.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1807 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1886
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009649 1887 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1950
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 350-519 2.55e-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: 2.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  350 HYISAEEEDWDYAPSVPT----SDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 425
Cdd:cd04229     3 YYIAAEEVDWDYAPSGKNkcclGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRAEVGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  426 TLLIIFKNQASR-PYNIYPHGITdVSPLHARRLPRGIKHVKdlpihPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFIN 504
Cdd:cd04229    83 TIKVVFKNNLDEfPVNMHPHGGL-YSKDNEGTTDGAGDVVA-----PGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHVD 156

                         170
                  ....*....|....*
gi 569009649  505 PERDLASGLIGPLLI 519
Cdd:cd04229   157 VFAHTNAGLVGPIIV 171
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1955-2103 4.27e-38

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: 139.95  E-value: 4.27e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   1955 CQIPLGMASgsirDFQITASGHYgqWAPNLARLHYsGSINAWSTKEP--FSWIKVDLLAPMIVHGIKTQGArqkFSSLYI 2032
Cdd:smart00231    2 CNEPLGLES----DSQITASSSY--WAAKIARLNG-GSDGGWCPAKNdlPPWIQVDLGRLRTVTGVITGRR---HGNGDW 71

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009649   2033 SQFIIMYSLDGKKWLSYQGnstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMGC 2103
Cdd:smart00231   72 VTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 350-522 1.05e-37

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: 140.36  E-value: 1.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  350 HYISAEEEDWDYAPSVPTSDNGSYKSQYLSngphrigrkYKKVRFIAYTDETFKTRET---IQHESGLLGPLLYGEVGDT 426
Cdd:cd14451     4 YYIAAEEEEWDYAGYGKSRLDKTQNERDTV---------FKKVVFRRYLDSTFSTPDIqgeYEEHLGILGPVIRAEVDDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  427 LLIIFKNQASRPYNIYPHGITDVSPLHARRL----PRGIKhvKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSF 502
Cdd:cd14451    75 IQVFFKNLASRPYSLHAHGLSYEKSSEGLSYddesPDWFK--KDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSA 152

                         170       180
                  ....*....|....*....|
gi 569009649  503 INPERDLASGLIGPLLICYK 522
Cdd:cd14451   153 VNPEKDIHSGLIGPLLICRK 172
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1807-1950 1.27e-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: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1807 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1886
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009649 1887 IQSIHFSGHVFTVRKkeeYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1950
Cdd:cd11021    81 IHSAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 350-522 1.49e-37

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: 139.61  E-value: 1.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  350 HYISAEEEDWDYAPsvptsdngsyksQYLSNGPHRIGRKYKKVRFIAYtDETFKTRETIQHESGLLGPLLYGEVGDTLLI 429
Cdd:cd04226     3 YYIAAQNIDWDYTP------------QSEELRLKRSEQSFKKIVYREY-EEGFKKEKPADLSSGLLGPTLRAEVGDTLIV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  430 IFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVK--DLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINPER 507
Cdd:cd04226    70 HFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEklDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVR 149

                         170
                  ....*....|....*
gi 569009649  508 DLASGLIGPLLICYK 522
Cdd:cd04226   150 DFNSGLIGALLICKK 164
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 5-147 6.70e-37

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: 138.09  E-value: 6.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649    5 FPFNTSIMYKKTVFVEYKDQLFN--IAKPRPPWMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYE 82
Cdd:cd14450    36 FSNNIGKKYKKAVFTQYEDGSFTkrLENPRPKEEGILGPVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYP 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569009649   83 DQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCK 147
Cdd:cd14450   116 PDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHSAVDITRDIASGLIGPLLICK 180
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 535-674 7.54e-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: 136.45  E-value: 7.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  535 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSL-ELTVCLHEVAYWHILSVGAQTD 613
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLpGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009649  614 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 674
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 535-677 2.02e-36

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: 135.30  E-value: 2.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  535 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTD 613
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPgLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009649  614 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 677
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1632-1792 3.21e-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: 136.40  E-value: 3.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1632 RHYFIAAVERLWDYGMSTSHVLRNR-YQSD--------NVPQ-----FKKVVFQEFTDGSFSQPLyrgELNEHLGLLGPY 1697
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQtFDDDehasvflkRGPDrigrvYKKAVYLQYTDDTYRTEI---EKPVWLGFLGPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1698 IRAEVEDNIMVTFKNQASRPYSFYSSLISYKEDQRGE---------EPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKA 1768
Cdd:cd04222    78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGAlypdntsgfEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                         170       180
                  ....*....|....*....|....
gi 569009649 1769 WAYFSDVDLERDMHSGLIGPLLIC 1792
Cdd:cd04222   158 RIYHSHIDAPKDIASGLIGPLIIC 181
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1632-1792 2.12e-34

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: 130.87  E-value: 2.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1632 RHYFIAAVERLWDYGMST--SHVLRNRYQSDNVPQ-FKKVVFQEFTDGSFSQPLYRGELnehLGLLGPYIRAEVEDNIMV 1708
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDlgDPASEQRKKPKDIPQkYIKAVFVEYLDATFTVPKPRPAW---MGLLGPTIVAEVGDTVVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1709 TFKNQASRPYSFYSSLISY--------KEDQ-RGEEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLER 1779
Cdd:cd14452    78 TFKNLASQPYSLHAVGVSYwkasegagYDDStSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVK 157

                         170
                  ....*....|...
gi 569009649 1780 DMHSGLIGPLLIC 1792
Cdd:cd14452   158 DVNSGLIGALLVC 170
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1808-1955 3.75e-34

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: 128.75  E-value: 3.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1808 QEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1887
Cdd:cd11022     2 KEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009649 1888 QSIHFSGHvfTVRKKEEYKMAVyNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVysKQC 1955
Cdd:cd11022    82 HGIYFSGN--TFLLQGTRRDTA-NLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV--SQC 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 13-149 5.61e-34

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 129.46  E-value: 5.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   13 YKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVHDTVVITLKN-MASHPVSLHAVGVSYWKASEGdeyedqtsQMEKE 91
Cdd:cd04229    46 YTKARYREYTDNSFSTPKPTPAYLGILGPVIRAEVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEG--------TTDGA 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 569009649   92 DDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCKEG 149
Cdd:cd04229   118 GDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 350-520 6.34e-34

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: 129.33  E-value: 6.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  350 HYISAEEEDWDYApsvpTSDNGSYKSQYLSNgPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGDTLLI 429
Cdd:cd14452     3 YYIAAVEIGWDYI----HSDLGDPASEQRKK-PKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGDTVVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  430 IFKNQASRPYNIYPHGIT-----------DVSPLHARrlprgikhvKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRY 498
Cdd:cd14452    78 TFKNLASQPYSLHAVGVSywkasegagydDSTSQHEK---------EDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYS 148

                         170       180
                  ....*....|....*....|..
gi 569009649  499 YSSFINPERDLASGLIGPLLIC 520
Cdd:cd14452   149 YSSQVDPVKDVNSGLIGALLVC 170
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2107-2260 1.89e-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: 126.86  E-value: 1.89e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   2107 SCSIPLGMESkvisDTQITASSyftnmfATWSPSQARLHlQGRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlf 2186
Cdd:smart00231    1 PCNEPLGLES----DSQITASS------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHG-- 67

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009649   2187 TSMFVKEFLISSSqDGHHWTqILYNGKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILGC 2260
Cdd:smart00231   68 NGDWVTYKLEYSD-DGVNWT-TYKDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 350-520 8.23e-33

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: 126.15  E-value: 8.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  350 HYISAEEEDWDYAPSVPTSdngSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFK---TRETIQHESGLLGPLLYGEVGDT 426
Cdd:cd04228     4 YFIAAVEVLWDYGMQRPQH---FLRARDPNRGRRKSVPQYKKVVFREYLDGSFTqpvYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  427 LLIIFKNQASRPYNIYPHGITDVSplHARRLPRGikhvkdLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINPE 506
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEE--DQRAEPRG------NFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLE 152

                         170
                  ....*....|....
gi 569009649  507 RDLASGLIGPLLIC 520
Cdd:cd04228   153 KDLHSGLIGPLIIC 166
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1630-1792 3.02e-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: 124.66  E-value: 3.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1630 KTRHYFIAAVERLWDYGMSTSHVLRNRYQS---DNVPQ-----FKKVVFQEFTDGSFSQplyRGELNEHLGLLGPYIRAE 1701
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSrylPTGPQrigykYKKVAFVEYTDKTFKR---REAKQTEKGILGPLLKGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1702 VEDNIMVTFKNQASRPYSFY----SSLISYK--EDQRGEEPRRNF-VKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSD 1774
Cdd:cd04227    78 VGDQIHIMFKNTASRPYNIYphglTSVRPMYrsRNPAGEKDLKTMpIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQST 157

                         170
                  ....*....|....*...
gi 569009649 1775 VDLERDMHSGLIGPLLIC 1792
Cdd:cd04227   158 VDPERDLASGLIGPLLIC 175
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 13-147 3.62e-32

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: 124.12  E-value: 3.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   13 YKKTVFVEYKDQLFNIAKPRPPWM---GLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSywkasegdeyEDQTSQME 89
Cdd:cd04225    48 YKKVVYREYTDDTFSVPKERTAEEehlGILGPLIHAEVGEKVKIVFKNMASRPYSIHAHGVK----------TDSSWVAP 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 569009649   90 KEddkvfPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCK 147
Cdd:cd04225   118 TE-----PGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYSGLIGPLVICR 170
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 1632-1792 3.85e-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: 121.12  E-value: 3.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1632 RHYFIAAVERLWDYGMSTSHVLRNRYQsdnvPQFKKVVFQEFTDGsFSQPLYRGELNehlGLLGPYIRAEVEDNIMVTFK 1711
Cdd:cd04226     1 REYYIAAQNIDWDYTPQSEELRLKRSE----QSFKKIVYREYEEG-FKKEKPADLSS---GLLGPTLRAEVGDTLIVHFK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1712 NQASRPYSFYSSLISYKEDQRGE---------EPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMH 1782
Cdd:cd04226    73 NMADKPLSIHPQGIAYGKKSEGSlysdntspvEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFN 152

                         170
                  ....*....|
gi 569009649 1783 SGLIGPLLIC 1792
Cdd:cd04226   153 SGLIGALLIC 162
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 13-149 4.81e-30

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: 118.07  E-value: 4.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   13 YKKTVFVEYKDQLFNIAKPR---PPWMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYwkasegdeYEDQTSQME 89
Cdd:cd04228    40 YKKVVFREYLDGSFTQPVYRgelDEHLGILGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISY--------EEDQRAEPR 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   90 KEddKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCKEG 149
Cdd:cd04228   112 GN--FVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1632-1791 6.07e-30

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 117.90  E-value: 6.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1632 RHYFIAAVERLWDYGMSTS---HVLRNRYQSDNVPQ---------FKKVVFQEFTDGSFSQPLyrgELNEHLGLLGPYIR 1699
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKnkcCLGDDLEVSTLDSQpgpytigstYTKARYREYTDNSFSTPK---PTPAYLGILGPVIR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1700 AEVEDNIMVTFKNQASR-PYSFYSSLISYKEDQRGEEPRRN-FVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDL 1777
Cdd:cd04229    78 AEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGAGdVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHVDV 157

                         170
                  ....*....|....
gi 569009649 1778 ERDMHSGLIGPLLI 1791
Cdd:cd04229   158 FAHTNAGLVGPIIV 171
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2123-2257 1.42e-29

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: 115.24  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  2123 QITASSYFTNmfaTWsPSQARLHLQGRTnAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlFTSMFVKEFLISSSQDG 2202
Cdd:pfam00754    1 QITASSSYSG---EG-PAAAALDGDPNT-AWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009649  2203 HHWTQIlyngKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIW--EHQIALRLEI 2257
Cdd:pfam00754   75 ENWTTV----KDEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWngGNGIALRAEL 127
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 13-147 9.18e-29

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: 114.64  E-value: 9.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   13 YKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSywkaSEGDEYEDQTSQMEKE- 91
Cdd:cd04227    44 YKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGDQIHIMFKNTASRPYNIYPHGLT----SVRPMYRSRNPAGEKDl 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009649   92 -DDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSHVDLVKDLNSGLIGALLVCK 147
Cdd:cd04227   120 kTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDPERDLASGLIGPLLICK 176
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 160-293 2.63e-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: 2.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  160 YQFVLLFAVFDEGKSWHSETN------DSYTQSMDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEI 233
Cdd:cd11021     2 REFVLMFSVVDENLSWYLDENiktycsEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  234 HSIFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 293
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.
 1970-2100 3.02e-26

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


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 105.61  E-value: 3.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  1970 QITASGHY-GQWAPNlARLHysGSIN-AWSTKE--PFSWIKVDLLAPMIVHGIKTQGaRQKFSSLYISQFIIMYSLDGKK 2045
Cdd:pfam00754    1 QITASSSYsGEGPAA-AALD--GDPNtAWSAWSgdDPQWIQVDLGKPKKITGVVTQG-RQDGSNGYVTSYKIEYSLDGEN 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009649  2046 WLSYQGNSTgtlmvfFGNVDSSGIKHNSFNPPIIARYIRLHPT--HSSIRSTLRMEL 2100
Cdd:pfam00754   77 WTTVKDEKI------PGNNDNNTPVTNTFDPPIKARYVRIVPTswNGGNGIALRAEL 127
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 161-296 3.52e-26

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: 106.03  E-value: 3.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  161 QFVLLFAVFDEGKSWHSETN-DSYTQSMDSASARDWP-----KMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 234
Cdd:cd11022     3 EFFLLFTVFDENESWYLDENiQQFTLDPRSVDKEDEDfqesnKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009649  235 SIFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKVDSC 296
Cdd:cd11022    83 GIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 536-674 1.10e-25

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: 104.95  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  536 KRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDF 614
Cdd:cd11012     2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQgLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009649  615 LSIFFSGYTF--KHKMVYE-DTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 674
Cdd:cd11012    82 HTAHFHGHSFdyKHRGVYRsDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 540-674 1.34e-24

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: 101.50  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  540 ILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDFLSIF 618
Cdd:cd11018     6 LLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPgLVMAQHQRIRWHLLNMGSDEEIHSVH 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009649  619 FSGYTF------KHKM-VYedtlTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 674
Cdd:cd11018    86 FHGLPFtvrakkEYRMgVY----NLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1808-1950 1.49e-23

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 98.44  E-value: 1.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1808 QEFALLFTIFDETKSWYFTENVKRNcktpcnfQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1887
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYSEVGERKS-------RDKFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009649 1888 QSIHFSGHVFTVRKkeeYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1950
Cdd:cd11015    75 HSIFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1812-1952 3.60e-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: 97.63  E-value: 3.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1812 LLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPgLVMAQDQRIRWYLLSMGNNENIQSIH 1891
Cdd:cd11016     6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009649 1892 FSGHVFtvrKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVYS 1952
Cdd:cd11016    85 FSGNTF---KHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVST 142
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1813-1930 1.30e-22

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


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 96.09  E-value: 1.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1813 LFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENIQSIHF 1892
Cdd:cd14454     7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 569009649 1893 SGHVFTVRKKEEykmAVYNLYPGVFETLEMIPSRAGIW 1930
Cdd:cd14454    87 SGHTFRYKGKHE---DTLNLFPMSGESITVTMDNLGTW 121
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 161-293 1.56e-21

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 92.23  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  161 QFVLLFAVFDEGKSWHSeTNDSyTQSMdsasardwpkMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFLEG 240
Cdd:cd14453     3 EYVLMFGVFDENKSWYK-QNAS-VDSV----------KYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNG 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 569009649  241 HTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 293
Cdd:cd14453    71 QVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 161-289 3.41e-20

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: 89.17  E-value: 3.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  161 QFVLLFAVFDEGKSWHSETN-DSYTQ-----SMDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 234
Cdd:cd11018     3 EFALLFTIFDETKSWYFEENmRRNCRppchiQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 569009649  235 SIFLEGHTFFVR---NHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEA 289
Cdd:cd11018    83 SVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSA 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1808-1950 4.91e-20

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 87.67  E-value: 4.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1808 QEFALLFTIFDEtkswyftENVKrncktpcnfqmedptlkENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1887
Cdd:cd11023     2 QEFIENSSIFLD-------LNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDF 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009649 1888 QSIHFSGHvfTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1950
Cdd:cd11023    58 HTPHWHGQ--TVEADKSRRTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1808-1944 5.05e-19

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: 84.91  E-value: 5.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1808 QEFALLFTIFDETKSWYFTENVKRNCKtpcnfqmedptlkenyrfHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1887
Cdd:cd14453     2 KEYVLMFGVFDENKSWYKQNASVDSVK------------------YTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009649 1888 QSIHFSGHVFtvrKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGM 1944
Cdd:cd14453    64 FSVHFNGQVL---EQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 161-293 7.54e-19

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: 85.31  E-value: 7.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  161 QFVLLFAVFDEGKSWHSETN-DSYTQSMDSASARDWP-----KMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 234
Cdd:cd11012     3 EFALLFLVFDENESWYLDENiKTYSDHPEKVNKEDEEfiesnKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009649  235 SIFLEGHTF-FVRN--HRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 293
Cdd:cd11012    83 TAHFHGHSFdYKHRgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 165-287 2.55e-18

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: 83.77  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  165 LFAVFDEGKSWHSETNDSYTQSMDSASARDWPK------MHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 238
Cdd:cd14454     7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKfyksniMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 569009649  239 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGM 287
Cdd:cd14454    87 SGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGL 135
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 539-674 2.41e-17

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: 80.68  E-value: 2.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  539 VILFSIFDENQSWYITENMQRflpNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDFLSIF 618
Cdd:cd14455     5 VLLFMTFDEEKSWYYEKNRKR---TCRENRVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVVH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569009649  619 FSGYTFKHKMVYEDTLTLFPF---SGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 674
Cdd:cd14455    82 FHGQTFTEKGLKDHQLGVYPLlpgSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 163-296 1.25e-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: 76.06  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  163 VLLFAVFDEGKSWHSETN-DSYTQSMDSASARDwPK------MHTVNGYVNRSLPGLIgCHRKSVYWHVIGMGTTPEIHS 235
Cdd:cd11016     5 SLLFSVFDENNSWYLKENiHRFTQTPAGVNDTD-PDfyasnvMHTINGIVFDRRQFVI-CLTDVAYWYVLSVGAQTDFLS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009649  236 IFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKVDSC 296
Cdd:cd11016    83 VFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 539-674 1.29e-15

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: 75.71  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  539 VILFSIFDENQSWYiTENMQRflpnaaKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDFLSI 617
Cdd:cd11015     5 VLLFAVFDEGKSWY-SEVGER------KSRDKFKRADSRKEFHTINGYINASLPgLKICQRKPVIWHVIGMGTAPEVHSI 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009649  618 FFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 674
Cdd:cd11015    78 FFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 161-289 2.99e-15

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: 74.90  E-value: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  161 QFVLLFAVFDEGKSWHSETNDSYT---QSMDSASARDWPKMHTVNGYVnRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIF 237
Cdd:cd14455     3 EFVLLFMTFDEEKSWYYEKNRKRTcreNRVKDPNVQDNHTFHAINGII-YNLKGLRMYTNELVRWHLINMGGPKDLHVVH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009649  238 LEGHTFF---VRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEA 289
Cdd:cd14455    82 FHGQTFTekgLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQT 136
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 535-674 4.03e-15

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: 73.74  E-value: 4.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  535 DKRNVILFSIFDENQSWYitenmqrflpnaaKTQPQDPgfqasNIMHSINGYVFDSL-ELTVCLHEVAYWHILSVGAQTD 613
Cdd:cd14453     1 YKEYVLMFGVFDENKSWY-------------KQNASVD-----SVKYTINGYTNGTLpDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009649  614 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 674
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 575-674 1.55e-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: 69.18  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  575 QASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDFLSIFFSGYTFK-HKMVYEDTLTLFPFSGETVFMSMENPG 652
Cdd:cd11023    17 EEAGLMHSINGYVFGNLPgVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEaDKSRRTDVAELMPASMRVADMTAADVG 96

                          90       100
                  ....*....|....*....|..
gi 569009649  653 LWVLGCHNSDFRKRGMTALLKV 674
Cdd:cd11023    97 TWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 198-287 1.39e-12

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: 66.48  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  198 MHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFLEGHTFFVRNHRQASL-EISPITFLTAQTLLIDLGQFLLF 276
Cdd:cd11023    22 MHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRTDVaELMPASMRVADMTAADVGTWLLH 101

                          90
                  ....*....|.
gi 569009649  277 CHISSHKHDGM 287
Cdd:cd11023   102 CHVHDHYMAGM 112
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 166-297 1.65e-12

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: 66.96  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   166 FAVFDEGKSWHSETNDSYTQSMDsASARDWPKM------HTVNGYVNRSLPGLIGCHRKSVYWHVIgMGTTPEIHSIFLE 239
Cdd:pfam00394    1 EDYVITLSDWYHKDAKDLEKELL-ASGKAPTDFppvpdaVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009649   240 GHTF--------FVRNHRQASLEISPITFLTAQ-TLLIDLGQFLLFCH-ISSHKHDGMEAYVKVDSCP 297
Cdd:pfam00394   79 GHKMtvvevdgvYVNPFTVDSLDIFPGQRYSVLvTANQDPGNYWIVASpNIPAFDNGTAAAILRYSGA 146
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 37-146 4.91e-11

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 61.92  E-value: 4.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   37 GLLGPTIWTEVHDTVVITLKN-MASHPVSLHAVGVSYWKASEGDEYEDQTSQMekeddkVFPGESHTYVWQVlkengpma 115
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQCP------IPPGESFTYRFTV-------- 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 569009649  116 sDPPCLTYSYMSHVDLvkDLNSGLIGALLVC 146
Cdd:cd04206    93 -DDQAGTFWYHSHVGG--QRADGLYGPLIVE 120
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1831-1954 2.18e-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: 60.53  E-value: 2.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  1831 RNCKTPCNFQMEDPTLkeNYRFHAINGYVMD-TLPGLVMAQDQRIRWYLLsmgNNENI-QSIHFSGHVFTV-----RKKE 1903
Cdd:pfam07731    2 TPPKLPTLLQITSGNF--RRNDWAINGLLFPpNTNVITLPYGTVVEWVLQ---NTTTGvHPFHLHGHSFQVlgrggGPWP 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009649  1904 EYKMAVYNL-----------YPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVYSKQ 1954
Cdd:pfam07731   77 EEDPKTYNLvdpvrrdtvqvPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 40-145 4.53e-07

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 50.73  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   40 GPTIWTEVHDTVVITLKNMASHPVSLHAVGVSywkasegDEYEDQTSQMEkeddkVFPGESHTYVWQvlkengpmaSDPP 119
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIH-------DAAMDGTGLGP-----IMPGESFTYEFV---------AEPA 90

                          90       100
                  ....*....|....*....|....*..
gi 569009649  120 ClTYSYMSHVDLVKD-LNSGLIGALLV 145
Cdd:cd11024    91 G-THLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 416-519 9.32e-07

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 49.78  E-value: 9.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  416 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVSPLHArrlpRGIKHVKDLPIHPGEIFKYKWtvtvedgptKSDPRCl 495
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKM----DGVPGVTQPAIEPGESFTYKF---------KAERPG- 96

                          90       100
                  ....*....|....*....|....*
gi 569009649  496 TRYYSSFIN-PERDLASGLIGPLLI 519
Cdd:cd13859    97 TLWYHCHVNvNEHVGMRGMWGPLIV 121
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 413-520 1.60e-06

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 49.21  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  413 GLLGPLLYGEVGDTLLIIFKNQ-ASRPYNIYPHGItdvsplharRLPR-----GIKHVKDLPIHPGEIFKYKWTVtvedg 486
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGL---------RQPGtndgdGVAGLTQCPIPPGESFTYRFTV----- 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569009649  487 ptksDPRCLTRYYSSFINPERdlASGLIGPLLIC 520
Cdd:cd04206    93 ----DDQAGTFWYHSHVGGQR--ADGLYGPLIVE 120
rpoC2 CHL00117
RNA polymerase beta'' subunit; Reviewed
 1081-1456 2.57e-05

RNA polymerase beta'' subunit; Reviewed


Pssm-ID: 214368 [Multi-domain]  Cd Length: 1364  Bit Score: 49.94  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1081 NGNNSLNSEQEHSPKQLVYLMFKKYVKNQSFLSEKNKVTVEqdgFTKNIGLKdmafphnmSIFLTTLSNVHENGRHNQEK 1160
Cdd:CHL00117  741 PGTGKKNSKESKKIKNWIYVQRITPTKKKYFVLVRPVVTYE---IADGINLA--------TLFPQDLLQEKDNLQLRVVN 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1161 NIQEEIEKEalIEEkvvlpqvheaTGSKNFLKDILILGTRQ---NISLYEVH---VPVLQNitsiNNSTNTVQIHM--EH 1232
Cdd:CHL00117  810 YILYGNGKP--IRG----------ISSIQLVRTCLVLNWDQdkkSSSIEEARasfVEVRTN----GLIRDFLRINLvkSP 873

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1233 FFKRRKDKETNSEGLVNKTremvKNYPSQKNIttqrskraLGQFRLSTQWLKTincsTQCIIKQI-DHSKEMKKFITKSS 1311
Cdd:CHL00117  874 ISYIRKRNDPSSSGLLVQS----NNFLDSTNI--------YSKAEIQSQSLSQ----NQGTIRTLlNRNKESQSLLILSS 937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1312 lSDSSVIKSTTQTNSSDSHIVKTSAFPPIDLKRSPFQNKFSHVQASSYIYDFKTKSSRIqesNNFLKETKINNPSLAILP 1391
Cdd:CHL00117  938 -SDCFRIGPFNGKKSKYHNIKESNPLIPIRNSLGPLGTVLQIANFSSSYHLLTHNQILV---TKYLQLDNLKQTFQVKVL 1013

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009649 1392 WNMFIDQ-GKFTSPgKSNTNSVTYKKRENIIFLKPTLPEESGKIELLPQvSIQEEEILPTETSHGS 1456
Cdd:CHL00117 1014 KYYLIDEnGKIYNP-DPCSNIILNPFNLNWYFLHHNYCEETSTIISLGQ-FICENVCISKNGPHKS 1077
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1839-1948 3.87e-05

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


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 45.53  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649 1839 FQMEDPTLKENYRFHAINGYVMDTLPG----LVMAQDQRIRWYLLSMGNNENIQSIHFSGHVFTV----------RKKEE 1904
Cdd:cd04207     6 LVLSQTGAPDGTTRWVINGMPFKEGDAntdiFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFWVlgsgggpfdaPLNLT 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 569009649 1905 YKMA--VYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLF 1948
Cdd:cd04207    86 NPPWrdTVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 399-519 8.09e-05

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


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 44.15  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  399 DETFKTRETIQHESGLLGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplharRLPR---GIKHVKDLPIHPGEIF 475
Cdd:cd13861    14 DLGGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL---------RLPNamdGVPGLTQPPVPPGESF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 569009649  476 KYKWTVtvedgPtksDPRclTRYYSSFINPERDLASGLIGPLLI 519
Cdd:cd13861    85 TYEFTP-----P---DAG--TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 416-519 1.02e-04

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: 43.79  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  416 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksdpr 493
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGL------FQNGTNwmDGTAGITQCPIPPGGSFTYNFTVDGQYG------- 96

                          90       100
                  ....*....|....*....|....*.
gi 569009649  494 clTRYYSSFINPErdLASGLIGPLLI 519
Cdd:cd13857    97 --TYWYHSHYSTQ--YADGLVGPLIV 118
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 416-519 2.19e-04

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


Pssm-ID: 259919 [Multi-domain]  Cd Length: 117  Bit Score: 42.67  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649  416 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksdpr 493
Cdd:cd13850    28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGI------LQRGTPwsDGVPGVTQWPIQPGGSFTYRWKAEDQYG------- 94

                          90       100
                  ....*....|....*....|....*.
gi 569009649  494 clTRYYSSFINPErdLASGLIGPLLI 519
Cdd:cd13850    95 --LYWYHSHYRGY--YMDGLYGPIYI 116
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 37-145 3.59e-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: 42.22  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   37 GLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQtsqmekedDKVFPGESHTYVWQVlkengpmas 116
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGLTQ--------PPVPPGESFTYEFTP--------- 90

                          90       100
                  ....*....|....*....|....*....
gi 569009649  117 dPPCLTYSYMSHVDLVKDLNSGLIGALLV 145
Cdd:cd13861    91 -PDAGTYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 40-145 6.30e-04

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: 41.47  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   40 GPTIWTEVHDTVVITLKNMASHPVSLHAVGVSywkaSEGDEYEDQT---SQMEkeddkVFPGESHTYVWQVLKENGpmas 116
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTagiTQCP-----IPPGGSFTYNFTVDGQYG---- 96

                          90       100
                  ....*....|....*....|....*....
gi 569009649  117 dppclTYSYMSHVDLvkDLNSGLIGALLV 145
Cdd:cd13857    97 -----TYWYHSHYST--QYADGLVGPLIV 118
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 387-486 8.94e-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: 44.34  E-value: 8.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   387 RKYK-KVRFIAYTdETFKTRETIQHESGLLGPLLYGEVGDTLLIIFKNQASrpYNIYPHgitdvspLHARRLPR-----G 460
Cdd:TIGR03389    4 RHYTfDVQEKNVT-RLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQ--YNVTIH-------WHGVRQLRngwadG 73

                           90       100
                   ....*....|....*....|....*.
gi 569009649   461 IKHVKDLPIHPGEIFKYKWTVTVEDG 486
Cdd:TIGR03389   74 PAYITQCPIQPGQSYVYNFTITGQRG 99
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 40-145 1.10e-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: 41.48  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   40 GPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGdeyedqtSQMEKEDdkVFPGESHTYVWQVLK----ENGPMA 115
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDG-------TGMNASI--VAPGDTRIYTWRTHGgyrrADGSWA 99

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569009649  116 SDPPClTYSYMSHV----DLVKDLNSGLIGALLV 145
Cdd:cd14449   100 EGTAG-YWHYHDHVfgteHGTEGLSRGLYGALIV 132
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 414-519 2.58e-03

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 39.92  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   414 LLGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksd 491
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL------QQRGTPwmDGVPGVTQCPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 569009649   492 prclTRYYSSFINPERdlASGLIGPLLI 519
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 416-482 2.69e-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: 39.95  E-value: 2.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569009649  416 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVSplharrlprgIKHVKDLPIHPGEIFKYKWTVT 482
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAA----------MDGTGLGPIMPGESFTYEFVAE 88
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 40-145 2.92e-03

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


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 39.74  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009649   40 GPTIWTEVHDTVVITLKN-MASHPVSLHAVGV----SYWkaSEGDEYEDQTSQMekeddkvfPGESHTYVWQVlkengpm 114
Cdd:cd13845    30 GPTIRATAGDTIVVELENkLPTEGVAIHWHGIrqrgTPW--ADGTASVSQCPIN--------PGETFTYQFVV------- 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 569009649  115 asDPPClTYSYMSHVDLVKdlNSGLIGALLV 145
Cdd:cd13845    93 --DRPG-TYFYHGHYGMQR--SAGLYGSLIV 118
 
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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