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Conserved domains on  [gi|569009645|ref|XP_006527853|]
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coagulation factor VIII isoform X2 [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 ...
 392-568 2.77e-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: 333.82  E-value: 2.77e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  392 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 471
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  472 TLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 551
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 569009645  552 ERDLASGLIGPLLICYK 568
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 15-195 5.87e-98

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: 312.68  E-value: 5.87e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   15 RRYYLGAVELSWNYIQSDLLSvlhtdsrfLPRMSTSFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVH 94
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGD--------PASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   95 DTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 174
Cdd:cd14452    73 DTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQ 152

                         170       180
                  ....*....|....*....|.
gi 569009645  175 VDLVKDLNSGLIGALLVCKEG 195
Cdd:cd14452   153 VDPVKDVNSGLIGALLVCRMG 173
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1677-1841 3.75e-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: 3.75e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1677 TRHYFIAAVERLWDYGMSTS-HVLR----NRYQSDNVPQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDN 1751
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPqHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1752 IMVTFKNQASRPYSFYSSLISYKEDQRGeEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMHSGL 1831
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQRA-EPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGL 159

                         170
                  ....*....|
gi 569009645 1832 IGPLLICHAN 1841
Cdd:cd04228   160 IGPLIICKTG 169
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1853-1996 1.76e-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: 1.76e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1853 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1932
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009645 1933 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1996
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 581-723 2.57e-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: 2.57e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  581 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDF 660
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009645  661 LSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 723
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 205-339 2.03e-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: 237.88  E-value: 2.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  205 LYQFVLLFAVFDEGKSWHSETNDSYTQSmDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 284
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRD-KFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009645  285 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 339
Cdd:cd11015    80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2157-2305 4.10e-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: 4.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 2157 PLGMESKvISDTQITASSYFTnmfATWSPSQARLHlqgRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSLFTSMF 2236
Cdd:cd00057     2 PLGMESG-LADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009645 2237 VKEFLISSSQDGHHWTQILYNGKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILG 2305
Cdd:cd00057    75 VTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2004-2148 1.45e-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: 172.92  E-value: 1.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 2004 PLGMASGsIRDFQITASGHYG-QWAPNLARLHysgSINAWSTKE--PFSWIKVDLLAPMIVHGIKTQGARQKFSSLYISQ 2080
Cdd:cd00057     2 PLGMESG-LADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009645 2081 FIIMYSLDGKKWLSYQGNstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMG 2148
Cdd:cd00057    78 YKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
rpoC2 super family cl33332
RNA polymerase beta'' subunit; Reviewed
 1127-1502 2.52e-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: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1127 NGNNSLNSEQEHSPKQLVYLMFKKYVKNQSFLSEKNKVTVEqdgFTKNIGLKdmafphnmSIFLTTLSNVHENGRHNQEK 1206
Cdd:CHL00117  741 PGTGKKNSKESKKIKNWIYVQRITPTKKKYFVLVRPVVTYE---IADGINLA--------TLFPQDLLQEKDNLQLRVVN 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1207 NIQEEIEKEalIEEkvvlpqvheaTGSKNFLKDILILGTRQ---NISLYEVH---VPVLQNitsiNNSTNTVQIHM--EH 1278
Cdd:CHL00117  810 YILYGNGKP--IRG----------ISSIQLVRTCLVLNWDQdkkSSSIEEARasfVEVRTN----GLIRDFLRINLvkSP 873

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1279 FFKRRKDKETNSEGLVNKTremvKNYPSQKNIttqrskraLGQFRLSTQWLKTincsTQCIIKQI-DHSKEMKKFITKSS 1357
Cdd:CHL00117  874 ISYIRKRNDPSSSGLLVQS----NNFLDSTNI--------YSKAEIQSQSLSQ----NQGTIRTLlNRNKESQSLLILSS 937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1358 lSDSSVIKSTTQTNSSDSHIVKTSAFPPIDLKRSPFQNKFSHVQASSYIYDFKTKSSRIqesNNFLKETKINNPSLAILP 1437
Cdd:CHL00117  938 -SDCFRIGPFNGKKSKYHNIKESNPLIPIRNSLGPLGTVLQIANFSSSYHLLTHNQILV---TKYLQLDNLKQTFQVKVL 1013

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009645 1438 WNMFIDQ-GKFTSPgKSNTNSVTYKKRENIIFLKPTLPEESGKIELLPQvSIQEEEILPTETSHGS 1502
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 ...
 392-568 2.77e-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: 333.82  E-value: 2.77e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  392 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 471
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  472 TLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 551
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 569009645  552 ERDLASGLIGPLLICYK 568
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 15-195 5.87e-98

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: 312.68  E-value: 5.87e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   15 RRYYLGAVELSWNYIQSDLLSvlhtdsrfLPRMSTSFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVH 94
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGD--------PASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   95 DTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 174
Cdd:cd14452    73 DTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQ 152

                         170       180
                  ....*....|....*....|.
gi 569009645  175 VDLVKDLNSGLIGALLVCKEG 195
Cdd:cd14452   153 VDPVKDVNSGLIGALLVCRMG 173
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1677-1841 3.75e-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: 3.75e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1677 TRHYFIAAVERLWDYGMSTS-HVLR----NRYQSDNVPQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDN 1751
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPqHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1752 IMVTFKNQASRPYSFYSSLISYKEDQRGeEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMHSGL 1831
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQRA-EPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGL 159

                         170
                  ....*....|
gi 569009645 1832 IGPLLICHAN 1841
Cdd:cd04228   160 IGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1853-1996 1.76e-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: 1.76e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1853 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1932
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009645 1933 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1996
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 581-723 2.57e-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: 2.57e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  581 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDF 660
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009645  661 LSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 723
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 205-339 2.03e-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: 237.88  E-value: 2.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  205 LYQFVLLFAVFDEGKSWHSETNDSYTQSmDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 284
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRD-KFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009645  285 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 339
Cdd:cd11015    80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2157-2305 4.10e-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: 4.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 2157 PLGMESKvISDTQITASSYFTnmfATWSPSQARLHlqgRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSLFTSMF 2236
Cdd:cd00057     2 PLGMESG-LADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009645 2237 VKEFLISSSQDGHHWTQILYNGKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILG 2305
Cdd:cd00057    75 VTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2004-2148 1.45e-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: 172.92  E-value: 1.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 2004 PLGMASGsIRDFQITASGHYG-QWAPNLARLHysgSINAWSTKE--PFSWIKVDLLAPMIVHGIKTQGARQKFSSLYISQ 2080
Cdd:cd00057     2 PLGMESG-LADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009645 2081 FIIMYSLDGKKWLSYQGNstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMG 2148
Cdd:cd00057    78 YKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2001-2149 4.36e-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: 4.36e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   2001 CQIPLGMASgsirDFQITASGHYgqWAPNLARLHYsGSINAWSTKEP--FSWIKVDLLAPMIVHGIKTQGArqkFSSLYI 2078
Cdd:smart00231    2 CNEPLGLES----DSQITASSSY--WAAKIARLNG-GSDGGWCPAKNdlPPWIQVDLGRLRTVTGVITGRR---HGNGDW 71

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009645   2079 SQFIIMYSLDGKKWLSYQGnstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMGC 2149
Cdd:smart00231   72 VTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2153-2306 1.93e-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: 1.93e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   2153 SCSIPLGMESkvisDTQITASSyftnmfATWSPSQARLHlQGRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlf 2232
Cdd:smart00231    1 PCNEPLGLES----DSQITASS------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHG-- 67

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009645   2233 TSMFVKEFLISSSqDGHHWTqILYNGKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILGC 2306
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.
 2169-2303 1.41e-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: 1.41e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  2169 QITASSYFTNmfaTWsPSQARLHLQGRTnAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlFTSMFVKEFLISSSQDG 2248
Cdd:pfam00754    1 QITASSSYSG---EG-PAAAALDGDPNT-AWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009645  2249 HHWTQIlyngKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIW--EHQIALRLEI 2303
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.
 2016-2146 2.96e-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: 2.96e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  2016 QITASGHY-GQWAPNlARLHysGSIN-AWSTKE--PFSWIKVDLLAPMIVHGIKTQGaRQKFSSLYISQFIIMYSLDGKK 2091
Cdd:pfam00754    1 QITASSSYsGEGPAA-AALD--GDPNtAWSAWSgdDPQWIQVDLGKPKKITGVVTQG-RQDGSNGYVTSYKIEYSLDGEN 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009645  2092 WLSYQGNSTgtlmvfFGNVDSSGIKHNSFNPPIIARYIRLHPT--HSSIRSTLRMEL 2146
Cdd:pfam00754   77 WTTVKDEKI------PGNNDNNTPVTNTFDPPIKARYVRIVPTswNGGNGIALRAEL 127
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 212-343 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 569009645   212 FAVFDEGKSWHSETNDSYTQSMDsASARDWPKM------HTVNGYVNRSLPGLIGCHRKSVYWHVIgMGTTPEIHSIFLE 285
Cdd:pfam00394    1 EDYVITLSDWYHKDAKDLEKELL-ASGKAPTDFppvpdaVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009645   286 GHTF--------FVRNHRQASLEISPITFLTAQ-TLLIDLGQFLLFCH-ISSHKHDGMEAYVKVDSCP 343
Cdd:pfam00394   79 GHKMtvvevdgvYVNPFTVDSLDIFPGQRYSVLvTANQDPGNYWIVASpNIPAFDNGTAAAILRYSGA 146
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1877-2000 2.23e-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: 2.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  1877 RNCKTPCNFQMEDPTLkeNYRFHAINGYVMD-TLPGLVMAQDQRIRWYLLsmgNNENI-QSIHFSGHVFTV-----RKKE 1949
Cdd:pfam07731    2 TPPKLPTLLQITSGNF--RRNDWAINGLLFPpNTNVITLPYGTVVEWVLQ---NTTTGvHPFHLHGHSFQVlgrggGPWP 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009645  1950 EYKMAVYNL-----------YPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVYSKQ 2000
Cdd:pfam07731   77 EEDPKTYNLvdpvrrdtvqvPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
rpoC2 CHL00117
RNA polymerase beta'' subunit; Reviewed
 1127-1502 2.52e-05

RNA polymerase beta'' subunit; Reviewed


Pssm-ID: 214368 [Multi-domain]  Cd Length: 1364  Bit Score: 49.94  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1127 NGNNSLNSEQEHSPKQLVYLMFKKYVKNQSFLSEKNKVTVEqdgFTKNIGLKdmafphnmSIFLTTLSNVHENGRHNQEK 1206
Cdd:CHL00117  741 PGTGKKNSKESKKIKNWIYVQRITPTKKKYFVLVRPVVTYE---IADGINLA--------TLFPQDLLQEKDNLQLRVVN 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1207 NIQEEIEKEalIEEkvvlpqvheaTGSKNFLKDILILGTRQ---NISLYEVH---VPVLQNitsiNNSTNTVQIHM--EH 1278
Cdd:CHL00117  810 YILYGNGKP--IRG----------ISSIQLVRTCLVLNWDQdkkSSSIEEARasfVEVRTN----GLIRDFLRINLvkSP 873

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1279 FFKRRKDKETNSEGLVNKTremvKNYPSQKNIttqrskraLGQFRLSTQWLKTincsTQCIIKQI-DHSKEMKKFITKSS 1357
Cdd:CHL00117  874 ISYIRKRNDPSSSGLLVQS----NNFLDSTNI--------YSKAEIQSQSLSQ----NQGTIRTLlNRNKESQSLLILSS 937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1358 lSDSSVIKSTTQTNSSDSHIVKTSAFPPIDLKRSPFQNKFSHVQASSYIYDFKTKSSRIqesNNFLKETKINNPSLAILP 1437
Cdd:CHL00117  938 -SDCFRIGPFNGKKSKYHNIKESNPLIPIRNSLGPLGTVLQIANFSSSYHLLTHNQILV---TKYLQLDNLKQTFQVKVL 1013

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009645 1438 WNMFIDQ-GKFTSPgKSNTNSVTYKKRENIIFLKPTLPEESGKIELLPQvSIQEEEILPTETSHGS 1502
Cdd:CHL00117 1014 KYYLIDEnGKIYNP-DPCSNIILNPFNLNWYFLHHNYCEETSTIISLGQ-FICENVCISKNGPHKS 1077
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 433-532 8.99e-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: 8.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   433 RKYK-KVRFIAYTdETFKTRETIQHESGLLGPLLYGEVGDTLLIIFKNQASrpYNIYPHgitdvspLHARRLPR-----G 506
Cdd:TIGR03389    4 RHYTfDVQEKNVT-RLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQ--YNVTIH-------WHGVRQLRngwadG 73

                           90       100
                   ....*....|....*....|....*.
gi 569009645   507 IKHVKDLPIHPGEIFKYKWTVTVEDG 532
Cdd:TIGR03389   74 PAYITQCPIQPGQSYVYNFTITGQRG 99
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 460-565 2.63e-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: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   460 LLGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksd 537
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL------QQRGTPwmDGVPGVTQCPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 569009645   538 prclTRYYSSFINPERdlASGLIGPLLI 565
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 ...
 392-568 2.77e-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: 333.82  E-value: 2.77e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  392 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 471
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  472 TLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 551
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 569009645  552 ERDLASGLIGPLLICYK 568
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 15-195 5.87e-98

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: 312.68  E-value: 5.87e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   15 RRYYLGAVELSWNYIQSDLLSvlhtdsrfLPRMSTSFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVH 94
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGD--------PASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   95 DTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 174
Cdd:cd14452    73 DTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQ 152

                         170       180
                  ....*....|....*....|.
gi 569009645  175 VDLVKDLNSGLIGALLVCKEG 195
Cdd:cd14452   153 VDPVKDVNSGLIGALLVCRMG 173
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1677-1841 3.75e-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: 3.75e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1677 TRHYFIAAVERLWDYGMSTS-HVLR----NRYQSDNVPQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDN 1751
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPqHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1752 IMVTFKNQASRPYSFYSSLISYKEDQRGeEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMHSGL 1831
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQRA-EPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGL 159

                         170
                  ....*....|
gi 569009645 1832 IGPLLICHAN 1841
Cdd:cd04228   160 IGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1853-1996 1.76e-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: 1.76e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1853 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1932
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009645 1933 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1996
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 15-194 1.65e-83

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: 271.59  E-value: 1.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   15 RRYYLGAVELSWNYIQSDLLsvlHTDSRFLPRMSTSFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVH 94
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLA---EKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAEVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   95 DTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 174
Cdd:cd04199    78 DTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSH 157

                         170       180
                  ....*....|....*....|
gi 569009645  175 VDLVKDLNSGLIGALLVCKE 194
Cdd:cd04199   158 VDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 394-568 1.04e-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: 1.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  394 WIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGDTL 473
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAEVGDTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  474 LIIFKNQASRPYNIYPHGITDVSPLHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 551
Cdd:cd04199    81 KVHFKNKASRPYSIHPHGVSYEKDSEGASYSdqTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHVDL 160

                         170
                  ....*....|....*..
gi 569009645  552 ERDLASGLIGPLLICYK 568
Cdd:cd04199   161 EKDINSGLIGPLLICKK 177
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 581-723 2.57e-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: 2.57e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  581 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDF 660
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009645  661 LSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 723
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 205-339 2.03e-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: 237.88  E-value: 2.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  205 LYQFVLLFAVFDEGKSWHSETNDSYTQSmDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 284
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRD-KFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009645  285 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 339
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 ...
 1678-1840 2.27e-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: 2.27e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1678 RHYFIAAVERLWDYGMSTSH--------VLRNRYQSDNVPQFKKVVFQEFTDGSFSQPlyrGELNEHLGLLGPYIRAEVE 1749
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAekdlsyrnQYLDNGPFRIGRSYKKVVYREYTDESFTTP---GPQPEHLGILGPTIRAEVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1750 DNIMVTFKNQASRPYSFYSSLISYKEDQRG---------EEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSD 1820
Cdd:cd04199    78 DTIKVHFKNKASRPYSIHPHGVSYEKDSEGasysdqtgpDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSH 157

                         170       180
                  ....*....|....*....|
gi 569009645 1821 VDLERDMHSGLIGPLLICHA 1840
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 ...
 392-566 5.22e-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: 5.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  392 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQH--ESGLLGPLLYGEV 469
Cdd:cd14450     1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRpkEEGILGPVIRAQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  470 GDTLLIIFKNQASRPYNIYPHGITdVSP-----LHARRLPRGIKHVKdlPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRY 544
Cdd:cd14450    81 RDTIKIVFKNKASRPYSIYPHGVT-VSKaaegaSYPPDPRGNETQNK--AVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                         170       180
                  ....*....|....*....|..
gi 569009645  545 YSSFINPERDLASGLIGPLLIC 566
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 ...
 1853-1996 2.87e-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: 212.27  E-value: 2.87e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1853 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1932
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009645 1933 IQSIHFSGHVFTVRKkeeYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1996
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 ...
 581-720 2.68e-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: 203.80  E-value: 2.68e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  581 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTD 659
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPgLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009645  660 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 720
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 ...
 15-195 1.10e-59

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: 202.78  E-value: 1.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   15 RRYYLGAVELSWNYI-QSDLLSVLHTDSrflprmstsfpfntsiMYKKTVFVEYKDQlFNIAKPRPPWMGLLGPTIWTEV 93
Cdd:cd04226     1 REYYIAAQNIDWDYTpQSEELRLKRSEQ----------------SFKKIVYREYEEG-FKKEKPADLSSGLLGPTLRAEV 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   94 HDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMS 173
Cdd:cd04226    64 GDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYS 143

                         170       180
                  ....*....|....*....|..
gi 569009645  174 HVDLVKDLNSGLIGALLVCKEG 195
Cdd:cd04226   144 HVNMVRDFNSGLIGALLICKKG 165
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 15-194 1.32e-55

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: 191.86  E-value: 1.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   15 RRYYLGAVELSWNYIQS--DLLSVLHTDSRflpRMSTSF----PFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPT 88
Cdd:cd04222     1 REYYIGIRETQWDYAPSgkNLITNQTFDDD---EHASVFlkrgPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   89 IWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLT 168
Cdd:cd04222    78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                         170       180
                  ....*....|....*....|....*.
gi 569009645  169 YSYMSHVDLVKDLNSGLIGALLVCKE 194
Cdd:cd04222   158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1677-1838 3.12e-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: 3.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1677 TRHYFIAAVERLWDY-GMSTSHVLRNRYQSDNVpqFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDNIMVT 1755
Cdd:cd14451     1 KRRYYIAAEEEEWDYaGYGKSRLDKTQNERDTV--FKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1756 FKNQASRPYSFYSSLISYKEDQRG-----EEP----RRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERD 1826
Cdd:cd14451    79 FKNLASRPYSLHAHGLSYEKSSEGlsyddESPdwfkKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKD 158

                         170
                  ....*....|..
gi 569009645 1827 MHSGLIGPLLIC 1838
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 ...
 207-339 8.79e-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: 188.00  E-value: 8.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  207 QFVLLFAVFDEGKSWHSETNDSYTQS------MDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 280
Cdd:cd04200     3 EFVLLFAVFDENKSWYLEDNIKRFCDnpekvdKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569009645  281 SIFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 339
Cdd:cd04200    83 SIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2157-2305 4.10e-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: 4.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 2157 PLGMESKvISDTQITASSYFTnmfATWSPSQARLHlqgRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSLFTSMF 2236
Cdd:cd00057     2 PLGMESG-LADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009645 2237 VKEFLISSSQDGHHWTQILYNGKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILG 2305
Cdd:cd00057    75 VTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 396-577 3.29e-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: 3.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  396 HYISAEEEDWDYAPS-------VPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHES---GLLGPLL 465
Cdd:cd04224     6 YFIAAEEIMWDYAPSgknlftgQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEehlGILGPVI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  466 YGEVGDTLLIIFKNQASRPYNIYPHGI-----TDVSPLHARRLPRGikhvkdLPIHPGEIFKYKWTVTVEDGPTKSDPRC 540
Cdd:cd04224    86 RAEVGDTIKVTFRNKASRPFSIQPHGVfyeknYEGAMYRDGDPSPG------SHVSPGETFTYEWTVPEGVGPTNQDPPC 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 569009645  541 LTRYYSSFINPERDLASGLIGPLLICYKESVDQRGNQ 577
Cdd:cd04224   160 LTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQ 196
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2004-2148 1.45e-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: 172.92  E-value: 1.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 2004 PLGMASGsIRDFQITASGHYG-QWAPNLARLHysgSINAWSTKE--PFSWIKVDLLAPMIVHGIKTQGARQKFSSLYISQ 2080
Cdd:cd00057     2 PLGMESG-LADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009645 2081 FIIMYSLDGKKWLSYQGNstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMG 2148
Cdd:cd00057    78 YKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1676-1851 7.62e-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: 7.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1676 KTRHYFIAAVERLWDYGMS----TSHVLRNRYQSDNVP-----------QFKKVVFQEFTDGSFSQPLYRGELNEHLGLL 1740
Cdd:cd04224     2 KVRHYFIAAEEIMWDYAPSgknlFTGQNLTAPGSDSEVffqrnetriggTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1741 GPYIRAEVEDNIMVTFKNQASRPYSFYSSLISYKEDQRGEEPRRNF------VKPNETKIYFWKVQHHMAPTEDEFDCKA 1814
Cdd:cd04224    82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDpspgshVSPGETFTYEWTVPEGVGPTNQDPPCLT 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 569009645 1815 WAYFSDVDLERDMHSGLIGPLLICHANTLNpAHGRQV 1851
Cdd:cd04224   162 YLYFSAVDPVRDTNSGLVGPLLVCKKGSLN-ANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 395-568 1.40e-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: 1.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  395 IHYISAEEEDWDYAPSV------PTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFktRETIQHES--GLLGPLLY 466
Cdd:cd04222     2 EYYIGIRETQWDYAPSGknlitnQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTY--RTEIEKPVwlGFLGPILK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  467 GEVGDTLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHV--KDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRY 544
Cdd:cd04222    80 AEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFekADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRI 159

                         170       180
                  ....*....|....*....|....
gi 569009645  545 YSSFINPERDLASGLIGPLLICYK 568
Cdd:cd04222   160 YHSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 14-203 1.54e-47

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: 169.19  E-value: 1.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   14 IRRYYLGAVELSWNYIQSDLLSVLHTDSRflPRMSTSFPF----NTSI--MYKKTVFVEYKDQLFNIAKPRPP---WMGL 84
Cdd:cd04224     3 VRHYFIAAEEIMWDYAPSGKNLFTGQNLT--APGSDSEVFfqrnETRIggTYWKVRYVEYTDATFTTRKHRSKeeeHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   85 LGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTsqmEKEDDKVFPGESHTYVWQVLKENGPMASDP 164
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGD---PSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 569009645  165 PCLTYSYMSHVDLVKDLNSGLIGALLVCKEGSLSKERTQ 203
Cdd:cd04224   158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQ 196
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 15-195 6.81e-47

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: 166.55  E-value: 6.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   15 RRYYLGAVELSWNY---IQSDLlsvlhtdsrflprMSTSFPFNTSimYKKTVFVEYKDQLFNIAKPRPPW---MGLLGPT 88
Cdd:cd14451     2 RRYYIAAEEEEWDYagyGKSRL-------------DKTQNERDTV--FKKVVFRRYLDSTFSTPDIQGEYeehLGILGPV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   89 IWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLT 168
Cdd:cd14451    67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRT 146

                         170       180
                  ....*....|....*....|....*..
gi 569009645  169 YSYMSHVDLVKDLNSGLIGALLVCKEG 195
Cdd:cd14451   147 WAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 395-568 8.37e-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: 8.37e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  395 IHYISAEEEDWDYAPSVPTSD------NGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETF---KTRETIQHESGLLGPLL 465
Cdd:cd04225     2 TYYIAAEEVEWDYSPQRTWEQelhnthEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFsvpKERTAEEEHLGILGPLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  466 YGEVGDTLLIIFKNQASRPYNIYPHGITDVSPLHArrlprgikhvkdlPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYY 545
Cdd:cd04225    82 HAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVA-------------PTEPGETQTYTWKIPERSGPGVEDSNCISWAY 148

                         170       180
                  ....*....|....*....|...
gi 569009645  546 SSFINPERDLASGLIGPLLICYK 568
Cdd:cd04225   149 YSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 17-193 1.16e-41

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: 151.95  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   17 YYLGAVELSWNYIQSdllSVLHTDSRFLPRMSTSFPFNTSIMYKKTVFVEYKDQLFN--IAKPRPPWMGLLGPTIWTEVH 94
Cdd:cd14450     5 YFIAAEEVIWDYAPS---IPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTkrLENPRPKEEGILGPVIRAQVR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   95 DTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 174
Cdd:cd14450    82 DTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHSA 161

                         170
                  ....*....|....*....
gi 569009645  175 VDLVKDLNSGLIGALLVCK 193
Cdd:cd14450   162 VDITRDIASGLIGPLLICK 180
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1680-1838 3.33e-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: 3.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1680 YFIAAVERLWDYGMSTSHVLRNRYQS---DNVPQF-----KKVVFQEFTDGSFSQPLYRGELNEhLGLLGPYIRAEVEDN 1751
Cdd:cd14450     5 YFIAAEEVIWDYAPSIPENMDKRYRSqylDNFSNNigkkyKKAVFTQYEDGSFTKRLENPRPKE-EGILGPVIRAQVRDT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1752 IMVTFKNQASRPYSFYSSLISYKEDQRG----EEPRRNF-----VKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVD 1822
Cdd:cd14450    84 IKIVFKNKASRPYSIYPHGVTVSKAAEGasypPDPRGNEtqnkaVQPGETYTYKWNILETDEPTARDPRCLTRMYHSAVD 163

                         170
                  ....*....|....*.
gi 569009645 1823 LERDMHSGLIGPLLIC 1838
Cdd:cd14450   164 ITRDIASGLIGPLLIC 179
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1678-1838 4.97e-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: 4.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1678 RHYFIAAVERLWDYGMSTS-----HVLRNRYQSDNV---------PQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPY 1743
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTweqelHNTHEESPGNAFlnkgdkfigSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1744 IRAEVEDNIMVTFKNQASRPYSFYSSLIsyKEDQrgeePRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDL 1823
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGV--KTDS----SWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQ 154

                         170
                  ....*....|....*
gi 569009645 1824 ERDMHSGLIGPLLIC 1838
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 ...
 1853-1996 5.09e-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: 145.78  E-value: 5.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1853 VQEFALLFTIFDETKSWYFTENVKRNCKtpcNFQMEDPTLKENYRFHAINGYVMDtLPGLVMAQDQRIRWYLLSMGNNEN 1932
Cdd:cd14455     1 RREFVLLFMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009645 1933 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1996
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 ...
 581-714 7.87e-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: 7.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  581 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTD 659
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSApLGFCHSEVVQWHISSVGTQDE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009645  660 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGM 714
Cdd:cd14454    81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGL 135
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1853-1996 1.28e-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: 1.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1853 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1932
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009645 1933 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1996
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 396-565 2.61e-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: 2.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  396 HYISAEEEDWDYAPSVPT----SDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 471
Cdd:cd04229     3 YYIAAEEVDWDYAPSGKNkcclGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRAEVGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  472 TLLIIFKNQASR-PYNIYPHGITdVSPLHARRLPRGIKHVKdlpihPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFIN 550
Cdd:cd04229    83 TIKVVFKNNLDEfPVNMHPHGGL-YSKDNEGTTDGAGDVVA-----PGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHVD 156

                         170
                  ....*....|....*
gi 569009645  551 PERDLASGLIGPLLI 565
Cdd:cd04229   157 VFAHTNAGLVGPIIV 171
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2001-2149 4.36e-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: 4.36e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   2001 CQIPLGMASgsirDFQITASGHYgqWAPNLARLHYsGSINAWSTKEP--FSWIKVDLLAPMIVHGIKTQGArqkFSSLYI 2078
Cdd:smart00231    2 CNEPLGLES----DSQITASSSY--WAAKIARLNG-GSDGGWCPAKNdlPPWIQVDLGRLRTVTGVITGRR---HGNGDW 71

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009645   2079 SQFIIMYSLDGKKWLSYQGnstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMGC 2149
Cdd:smart00231   72 VTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1853-1996 1.10e-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: 139.14  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1853 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1932
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009645 1933 IQSIHFSGHVFTVRKkeeYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1996
Cdd:cd11021    81 IHSAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 396-568 1.10e-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: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  396 HYISAEEEDWDYAPSVPTSDNGSYKSQYLSngphrigrkYKKVRFIAYTDETFKTRET---IQHESGLLGPLLYGEVGDT 472
Cdd:cd14451     4 YYIAAEEEEWDYAGYGKSRLDKTQNERDTV---------FKKVVFRRYLDSTFSTPDIqgeYEEHLGILGPVIRAEVDDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  473 LLIIFKNQASRPYNIYPHGITDVSPLHARRL----PRGIKhvKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSF 548
Cdd:cd14451    75 IQVFFKNLASRPYSLHAHGLSYEKSSEGLSYddesPDWFK--KDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSA 152

                         170       180
                  ....*....|....*....|
gi 569009645  549 INPERDLASGLIGPLLICYK 568
Cdd:cd14451   153 VNPEKDIHSGLIGPLLICRK 172
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 396-568 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 569009645  396 HYISAEEEDWDYAPsvptsdngsyksQYLSNGPHRIGRKYKKVRFIAYtDETFKTRETIQHESGLLGPLLYGEVGDTLLI 475
Cdd:cd04226     3 YYIAAQNIDWDYTP------------QSEELRLKRSEQSFKKIVYREY-EEGFKKEKPADLSSGLLGPTLRAEVGDTLIV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  476 IFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVK--DLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINPER 553
Cdd:cd04226    70 HFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEklDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVR 149

                         170
                  ....*....|....*
gi 569009645  554 DLASGLIGPLLICYK 568
Cdd:cd04226   150 DFNSGLIGALLICKK 164
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 15-195 1.67e-37

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 139.86  E-value: 1.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   15 RRYYLGAVELSWNYIQSDLLSVLHTD--SRFLPRMSTSfPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTE 92
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKNKCCLGDdlEVSTLDSQPG-PYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   93 VHDTVVITLKN-MASHPVSLHAVGVSYWKASEGdeyedqtsQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSY 171
Cdd:cd04229    80 VGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEG--------TTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLY 151

                         170       180
                  ....*....|....*....|....
gi 569009645  172 MSHVDLVKDLNSGLIGALLVCKEG 195
Cdd:cd04229   152 HSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 581-720 6.59e-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: 136.83  E-value: 6.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  581 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSL-ELTVCLHEVAYWHILSVGAQTD 659
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLpGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009645  660 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 720
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 581-723 1.84e-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: 135.69  E-value: 1.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  581 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTD 659
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPgLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009645  660 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 723
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1678-1838 3.22e-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: 3.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1678 RHYFIAAVERLWDYGMSTSHVLRNR-YQSD--------NVPQ-----FKKVVFQEFTDGSFSQPLyrgELNEHLGLLGPY 1743
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQtFDDDehasvflkRGPDrigrvYKKAVYLQYTDDTYRTEI---EKPVWLGFLGPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1744 IRAEVEDNIMVTFKNQASRPYSFYSSLISYKEDQRGE---------EPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKA 1814
Cdd:cd04222    78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGAlypdntsgfEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                         170       180
                  ....*....|....*....|....
gi 569009645 1815 WAYFSDVDLERDMHSGLIGPLLIC 1838
Cdd:cd04222   158 RIYHSHIDAPKDIASGLIGPLIIC 181
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1678-1838 2.39e-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: 130.48  E-value: 2.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1678 RHYFIAAVERLWDYGMST--SHVLRNRYQSDNVPQ-FKKVVFQEFTDGSFSQPLYRGELnehLGLLGPYIRAEVEDNIMV 1754
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDlgDPASEQRKKPKDIPQkYIKAVFVEYLDATFTVPKPRPAW---MGLLGPTIVAEVGDTVVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1755 TFKNQASRPYSFYSSLISY--------KEDQ-RGEEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLER 1825
Cdd:cd14452    78 TFKNLASQPYSLHAVGVSYwkasegagYDDStSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVK 157

                         170
                  ....*....|...
gi 569009645 1826 DMHSGLIGPLLIC 1838
Cdd:cd14452   158 DVNSGLIGALLVC 170
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1854-2001 3.31e-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: 129.14  E-value: 3.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1854 QEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1933
Cdd:cd11022     2 KEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009645 1934 QSIHFSGHvfTVRKKEEYKMAVyNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVysKQC 2001
Cdd:cd11022    82 HGIYFSGN--TFLLQGTRRDTA-NLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV--SQC 144
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 15-193 5.00e-34

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 129.51  E-value: 5.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   15 RRYYLGAVELSWNYIQS----DLLSVLHTDSRFLPRMSTSFPFNTSiMYKKTVFVEYKDQLFNIAKPRPPWM---GLLGP 87
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQrtweQELHNTHEESPGNAFLNKGDKFIGS-KYKKVVYREYTDDTFSVPKERTAEEehlGILGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   88 TIWTEVHDTVVITLKNMASHPVSLHAVGVSywkasegdeyEDQTSQMEKEddkvfPGESHTYVWQVLKENGPMASDPPCL 167
Cdd:cd04225    80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVK----------TDSSWVAPTE-----PGETQTYTWKIPERSGPGVEDSNCI 144

                         170       180
                  ....*....|....*....|....*.
gi 569009645  168 TYSYMSHVDLVKDLNSGLIGALLVCK 193
Cdd:cd04225   145 SWAYYSTVDQIKDLYSGLIGPLVICR 170
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 14-195 5.66e-34

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 129.24  E-value: 5.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   14 IRRYYLGAVELSWNYIQSDLLSVLHtdSRFLPR-MSTSFPfntsiMYKKTVFVEYKDQLFNIAKPR---PPWMGLLGPTI 89
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPQHFLR--ARDPNRgRRKSVP-----QYKKVVFREYLDGSFTQPVYRgelDEHLGILGPYI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   90 WTEVHDTVVITLKNMASHPVSLHAVGVSYwkasegdeYEDQTSQMEKEddKVFPGESHTYVWQVLKENGPMASDPPCLTY 169
Cdd:cd04228    74 RAEVEDNIMVTFKNLASRPYSFHSSLISY--------EEDQRAEPRGN--FVQPGEVQTYSWKVLHQMAPTKQEFDCKAW 143

                         170       180
                  ....*....|....*....|....*.
gi 569009645  170 SYMSHVDLVKDLNSGLIGALLVCKEG 195
Cdd:cd04228   144 AYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 396-566 7.27e-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: 7.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  396 HYISAEEEDWDYApsvpTSDNGSYKSQYLSNgPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGDTLLI 475
Cdd:cd14452     3 YYIAAVEIGWDYI----HSDLGDPASEQRKK-PKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGDTVVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  476 IFKNQASRPYNIYPHGIT-----------DVSPLHARrlprgikhvKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRY 544
Cdd:cd14452    78 TFKNLASQPYSLHAVGVSywkasegagydDSTSQHEK---------EDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYS 148

                         170       180
                  ....*....|....*....|..
gi 569009645  545 YSSFINPERDLASGLIGPLLIC 566
Cdd:cd14452   149 YSSQVDPVKDVNSGLIGALLVC 170
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2153-2306 1.93e-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: 1.93e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   2153 SCSIPLGMESkvisDTQITASSyftnmfATWSPSQARLHlQGRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlf 2232
Cdd:smart00231    1 PCNEPLGLES----DSQITASS------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHG-- 67

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009645   2233 TSMFVKEFLISSSqDGHHWTqILYNGKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILGC 2306
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 ...
 396-566 8.65e-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: 8.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  396 HYISAEEEDWDYAPSVPTSdngSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFK---TRETIQHESGLLGPLLYGEVGDT 472
Cdd:cd04228     4 YFIAAVEVLWDYGMQRPQH---FLRARDPNRGRRKSVPQYKKVVFREYLDGSFTqpvYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  473 LLIIFKNQASRPYNIYPHGITDVSplHARRLPRGikhvkdLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINPE 552
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEE--DQRAEPRG------NFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLE 152

                         170
                  ....*....|....
gi 569009645  553 RDLASGLIGPLLIC 566
Cdd:cd04228   153 KDLHSGLIGPLIIC 166
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 17-193 2.78e-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: 125.04  E-value: 2.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   17 YYLGAVELSWNYiqSDLLSVlHTDSRFLPRMSTSFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVHDT 96
Cdd:cd04227     5 HYIAAEELDWDY--APLLSS-TDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGDQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   97 VVITLKNMASHPVSLHAVGVSywkaSEGDEYEDQTSQMEKE--DDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 174
Cdd:cd04227    82 IHIMFKNTASRPYNIYPHGLT----SVRPMYRSRNPAGEKDlkTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQST 157

                         170
                  ....*....|....*....
gi 569009645  175 VDLVKDLNSGLIGALLVCK 193
Cdd:cd04227   158 VDPERDLASGLIGPLLICK 176
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1676-1838 3.15e-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: 3.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1676 KTRHYFIAAVERLWDYGMSTSHVLRNRYQS---DNVPQ-----FKKVVFQEFTDGSFSQplyRGELNEHLGLLGPYIRAE 1747
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSrylPTGPQrigykYKKVAFVEYTDKTFKR---REAKQTEKGILGPLLKGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1748 VEDNIMVTFKNQASRPYSFY----SSLISYK--EDQRGEEPRRNF-VKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSD 1820
Cdd:cd04227    78 VGDQIHIMFKNTASRPYNIYphglTSVRPMYrsRNPAGEKDLKTMpIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQST 157

                         170
                  ....*....|....*...
gi 569009645 1821 VDLERDMHSGLIGPLLIC 1838
Cdd:cd04227   158 VDPERDLASGLIGPLLIC 175
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 1678-1838 3.89e-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: 3.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1678 RHYFIAAVERLWDYGMSTSHVLRNRYQsdnvPQFKKVVFQEFTDGsFSQPLYRGELNehlGLLGPYIRAEVEDNIMVTFK 1757
Cdd:cd04226     1 REYYIAAQNIDWDYTPQSEELRLKRSE----QSFKKIVYREYEEG-FKKEKPADLSS---GLLGPTLRAEVGDTLIVHFK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1758 NQASRPYSFYSSLISYKEDQRGE---------EPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMH 1828
Cdd:cd04226    73 NMADKPLSIHPQGIAYGKKSEGSlysdntspvEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFN 152

                         170
                  ....*....|
gi 569009645 1829 SGLIGPLLIC 1838
Cdd:cd04226   153 SGLIGALLIC 162
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1678-1837 6.19e-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: 6.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1678 RHYFIAAVERLWDYGMSTS---HVLRNRYQSDNVPQ---------FKKVVFQEFTDGSFSQPLyrgELNEHLGLLGPYIR 1745
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKnkcCLGDDLEVSTLDSQpgpytigstYTKARYREYTDNSFSTPK---PTPAYLGILGPVIR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1746 AEVEDNIMVTFKNQASR-PYSFYSSLISYKEDQRGEEPRRN-FVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDL 1823
Cdd:cd04229    78 AEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGAGdVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHVDV 157

                         170
                  ....*....|....
gi 569009645 1824 ERDMHSGLIGPLLI 1837
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.
 2169-2303 1.41e-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: 1.41e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  2169 QITASSYFTNmfaTWsPSQARLHLQGRTnAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlFTSMFVKEFLISSSQDG 2248
Cdd:pfam00754    1 QITASSSYSG---EG-PAAAALDGDPNT-AWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009645  2249 HHWTQIlyngKVKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIW--EHQIALRLEI 2303
Cdd:pfam00754   75 ENWTTV----KDEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWngGNGIALRAEL 127
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 206-339 2.42e-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: 2.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  206 YQFVLLFAVFDEGKSWHSETN------DSYTQSMDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEI 279
Cdd:cd11021     2 REFVLMFSVVDENLSWYLDENiktycsEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  280 HSIFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 339
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.
 2016-2146 2.96e-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: 2.96e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  2016 QITASGHY-GQWAPNlARLHysGSIN-AWSTKE--PFSWIKVDLLAPMIVHGIKTQGaRQKFSSLYISQFIIMYSLDGKK 2091
Cdd:pfam00754    1 QITASSSYsGEGPAA-AALD--GDPNtAWSAWSgdDPQWIQVDLGKPKKITGVVTQG-RQDGSNGYVTSYKIEYSLDGEN 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009645  2092 WLSYQGNSTgtlmvfFGNVDSSGIKHNSFNPPIIARYIRLHPT--HSSIRSTLRMEL 2146
Cdd:pfam00754   77 WTTVKDEKI------PGNNDNNTPVTNTFDPPIKARYVRIVPTswNGGNGIALRAEL 127
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 207-342 3.26e-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: 106.41  E-value: 3.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  207 QFVLLFAVFDEGKSWHSETN-DSYTQSMDSASARDWP-----KMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 280
Cdd:cd11022     3 EFFLLFTVFDENESWYLDENiQQFTLDPRSVDKEDEDfqesnKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009645  281 SIFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKVDSC 342
Cdd:cd11022    83 GIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 582-720 1.11e-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: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  582 KRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDF 660
Cdd:cd11012     2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQgLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009645  661 LSIFFSGYTF--KHKMVYE-DTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 720
Cdd:cd11012    82 HTAHFHGHSFdyKHRGVYRsDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 586-720 1.38e-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: 1.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  586 ILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDFLSIF 664
Cdd:cd11018     6 LLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPgLVMAQHQRIRWHLLNMGSDEEIHSVH 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009645  665 FSGYTF------KHKM-VYedtlTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 720
Cdd:cd11018    86 FHGLPFtvrakkEYRMgVY----NLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1854-1996 1.51e-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: 1.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1854 QEFALLFTIFDETKSWYFTENVKRNcktpcnfQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1933
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYSEVGERKS-------RDKFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009645 1934 QSIHFSGHVFTVRKkeeYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1996
Cdd:cd11015    75 HSIFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1858-1998 3.43e-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: 3.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1858 LLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPgLVMAQDQRIRWYLLSMGNNENIQSIH 1937
Cdd:cd11016     6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009645 1938 FSGHVFtvrKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVYS 1998
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 ...
 1859-1976 1.21e-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: 1.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1859 LFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENIQSIHF 1938
Cdd:cd14454     7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 569009645 1939 SGHVFTVRKKEEykmAVYNLYPGVFETLEMIPSRAGIW 1976
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 ...
 207-339 1.50e-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: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  207 QFVLLFAVFDEGKSWHSeTNDSyTQSMdsasardwpkMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFLEG 286
Cdd:cd14453     3 EYVLMFGVFDENKSWYK-QNAS-VDSV----------KYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNG 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 569009645  287 HTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 339
Cdd:cd14453    71 QVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 207-335 3.55e-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: 3.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  207 QFVLLFAVFDEGKSWHSETN-DSYTQ-----SMDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 280
Cdd:cd11018     3 EFALLFTIFDETKSWYFEENmRRNCRppchiQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 569009645  281 SIFLEGHTFFVR---NHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEA 335
Cdd:cd11018    83 SVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSA 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1854-1996 5.16e-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: 5.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1854 QEFALLFTIFDEtkswyftENVKrncktpcnfqmedptlkENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1933
Cdd:cd11023     2 QEFIENSSIFLD-------LNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDF 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009645 1934 QSIHFSGHvfTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 1996
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 ...
 1854-1990 4.96e-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: 4.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1854 QEFALLFTIFDETKSWYFTENVKRNCKtpcnfqmedptlkenyrfHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1933
Cdd:cd14453     2 KEYVLMFGVFDENKSWYKQNASVDSVK------------------YTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009645 1934 QSIHFSGHVFtvrKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGM 1990
Cdd:cd14453    64 FSVHFNGQVL---EQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 207-339 7.70e-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: 7.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  207 QFVLLFAVFDEGKSWHSETN-DSYTQSMDSASARDWP-----KMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 280
Cdd:cd11012     3 EFALLFLVFDENESWYLDENiKTYSDHPEKVNKEDEEfiesnKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009645  281 SIFLEGHTF-FVRN--HRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 339
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 ...
 211-333 2.46e-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: 2.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  211 LFAVFDEGKSWHSETNDSYTQSMDSASARDWPK------MHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 284
Cdd:cd14454     7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKfyksniMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 569009645  285 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGM 333
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 ...
 585-720 2.39e-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: 2.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  585 VILFSIFDENQSWYITENMQRflpNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDFLSIF 664
Cdd:cd14455     5 VLLFMTFDEEKSWYYEKNRKR---TCRENRVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVVH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569009645  665 FSGYTFKHKMVYEDTLTLFPF---SGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 720
Cdd:cd14455    82 FHGQTFTEKGLKDHQLGVYPLlpgSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 209-342 1.20e-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: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  209 VLLFAVFDEGKSWHSETN-DSYTQSMDSASARDwPK------MHTVNGYVNRSLPGLIgCHRKSVYWHVIGMGTTPEIHS 281
Cdd:cd11016     5 SLLFSVFDENNSWYLKENiHRFTQTPAGVNDTD-PDfyasnvMHTINGIVFDRRQFVI-CLTDVAYWYVLSVGAQTDFLS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009645  282 IFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKVDSC 342
Cdd:cd11016    83 VFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 585-720 1.31e-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: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  585 VILFSIFDENQSWYiTENMQRflpnaaKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDFLSI 663
Cdd:cd11015     5 VLLFAVFDEGKSWY-SEVGER------KSRDKFKRADSRKEFHTINGYINASLPgLKICQRKPVIWHVIGMGTAPEVHSI 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009645  664 FFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 720
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 ...
 207-335 3.05e-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: 3.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  207 QFVLLFAVFDEGKSWHSETNDSYT---QSMDSASARDWPKMHTVNGYVnRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIF 283
Cdd:cd14455     3 EFVLLFMTFDEEKSWYYEKNRKRTcreNRVKDPNVQDNHTFHAINGII-YNLKGLRMYTNELVRWHLINMGGPKDLHVVH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009645  284 LEGHTFF---VRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEA 335
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 ...
 581-720 3.96e-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: 3.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  581 DKRNVILFSIFDENQSWYitenmqrflpnaaKTQPQDPgfqasNIMHSINGYVFDSL-ELTVCLHEVAYWHILSVGAQTD 659
Cdd:cd14453     1 YKEYVLMFGVFDENKSWY-------------KQNASVD-----SVKYTINGYTNGTLpDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009645  660 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 720
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 621-720 1.66e-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: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  621 QASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDFLSIFFSGYTFK-HKMVYEDTLTLFPFSGETVFMSMENPG 698
Cdd:cd11023    17 EEAGLMHSINGYVFGNLPgVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEaDKSRRTDVAELMPASMRVADMTAADVG 96

                          90       100
                  ....*....|....*....|..
gi 569009645  699 LWVLGCHNSDFRKRGMTALLKV 720
Cdd:cd11023    97 TWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 244-333 1.46e-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: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  244 MHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFLEGHTFFVRNHRQASL-EISPITFLTAQTLLIDLGQFLLF 322
Cdd:cd11023    22 MHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRTDVaELMPASMRVADMTAADVGTWLLH 101

                          90
                  ....*....|.
gi 569009645  323 CHISSHKHDGM 333
Cdd:cd11023   102 CHVHDHYMAGM 112
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 212-343 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 569009645   212 FAVFDEGKSWHSETNDSYTQSMDsASARDWPKM------HTVNGYVNRSLPGLIGCHRKSVYWHVIgMGTTPEIHSIFLE 285
Cdd:pfam00394    1 EDYVITLSDWYHKDAKDLEKELL-ASGKAPTDFppvpdaVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009645   286 GHTF--------FVRNHRQASLEISPITFLTAQ-TLLIDLGQFLLFCH-ISSHKHDGMEAYVKVDSCP 343
Cdd:pfam00394   79 GHKMtvvevdgvYVNPFTVDSLDIFPGQRYSVLvTANQDPGNYWIVASpNIPAFDNGTAAAILRYSGA 146
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 83-192 4.92e-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: 4.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   83 GLLGPTIWTEVHDTVVITLKN-MASHPVSLHAVGVSYWKASEGDEYEDQTSQMekeddkVFPGESHTYVWQVlkengpma 161
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQCP------IPPGESFTYRFTV-------- 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 569009645  162 sDPPCLTYSYMSHVDLvkDLNSGLIGALLVC 192
Cdd:cd04206    93 -DDQAGTFWYHSHVGG--QRADGLYGPLIVE 120
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1877-2000 2.23e-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: 2.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  1877 RNCKTPCNFQMEDPTLkeNYRFHAINGYVMD-TLPGLVMAQDQRIRWYLLsmgNNENI-QSIHFSGHVFTV-----RKKE 1949
Cdd:pfam07731    2 TPPKLPTLLQITSGNF--RRNDWAINGLLFPpNTNVITLPYGTVVEWVLQ---NTTTGvHPFHLHGHSFQVlgrggGPWP 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009645  1950 EYKMAVYNL-----------YPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVYSKQ 2000
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 ...
 86-191 4.49e-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: 4.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   86 GPTIWTEVHDTVVITLKNMASHPVSLHAVGVSywkasegDEYEDQTSQMEkeddkVFPGESHTYVWQvlkengpmaSDPP 165
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIH-------DAAMDGTGLGP-----IMPGESFTYEFV---------AEPA 90

                          90       100
                  ....*....|....*....|....*..
gi 569009645  166 ClTYSYMSHVDLVKD-LNSGLIGALLV 191
Cdd:cd11024    91 G-THLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 462-565 8.30e-07

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 50.17  E-value: 8.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  462 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVSPLHArrlpRGIKHVKDLPIHPGEIFKYKWtvtvedgptKSDPRCl 541
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKM----DGVPGVTQPAIEPGESFTYKF---------KAERPG- 96

                          90       100
                  ....*....|....*....|....*
gi 569009645  542 TRYYSSFIN-PERDLASGLIGPLLI 565
Cdd:cd13859    97 TLWYHCHVNvNEHVGMRGMWGPLIV 121
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 459-566 1.57e-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: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  459 GLLGPLLYGEVGDTLLIIFKNQ-ASRPYNIYPHGItdvsplharRLPR-----GIKHVKDLPIHPGEIFKYKWTVtvedg 532
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGL---------RQPGtndgdGVAGLTQCPIPPGESFTYRFTV----- 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569009645  533 ptksDPRCLTRYYSSFINPERdlASGLIGPLLIC 566
Cdd:cd04206    93 ----DDQAGTFWYHSHVGGQR--ADGLYGPLIVE 120
rpoC2 CHL00117
RNA polymerase beta'' subunit; Reviewed
 1127-1502 2.52e-05

RNA polymerase beta'' subunit; Reviewed


Pssm-ID: 214368 [Multi-domain]  Cd Length: 1364  Bit Score: 49.94  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1127 NGNNSLNSEQEHSPKQLVYLMFKKYVKNQSFLSEKNKVTVEqdgFTKNIGLKdmafphnmSIFLTTLSNVHENGRHNQEK 1206
Cdd:CHL00117  741 PGTGKKNSKESKKIKNWIYVQRITPTKKKYFVLVRPVVTYE---IADGINLA--------TLFPQDLLQEKDNLQLRVVN 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1207 NIQEEIEKEalIEEkvvlpqvheaTGSKNFLKDILILGTRQ---NISLYEVH---VPVLQNitsiNNSTNTVQIHM--EH 1278
Cdd:CHL00117  810 YILYGNGKP--IRG----------ISSIQLVRTCLVLNWDQdkkSSSIEEARasfVEVRTN----GLIRDFLRINLvkSP 873

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1279 FFKRRKDKETNSEGLVNKTremvKNYPSQKNIttqrskraLGQFRLSTQWLKTincsTQCIIKQI-DHSKEMKKFITKSS 1357
Cdd:CHL00117  874 ISYIRKRNDPSSSGLLVQS----NNFLDSTNI--------YSKAEIQSQSLSQ----NQGTIRTLlNRNKESQSLLILSS 937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1358 lSDSSVIKSTTQTNSSDSHIVKTSAFPPIDLKRSPFQNKFSHVQASSYIYDFKTKSSRIqesNNFLKETKINNPSLAILP 1437
Cdd:CHL00117  938 -SDCFRIGPFNGKKSKYHNIKESNPLIPIRNSLGPLGTVLQIANFSSSYHLLTHNQILV---TKYLQLDNLKQTFQVKVL 1013

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009645 1438 WNMFIDQ-GKFTSPgKSNTNSVTYKKRENIIFLKPTLPEESGKIELLPQvSIQEEEILPTETSHGS 1502
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 ...
 1885-1994 3.84e-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: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645 1885 FQMEDPTLKENYRFHAINGYVMDTLPG----LVMAQDQRIRWYLLSMGNNENIQSIHFSGHVFTV----------RKKEE 1950
Cdd:cd04207     6 LVLSQTGAPDGTTRWVINGMPFKEGDAntdiFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFWVlgsgggpfdaPLNLT 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 569009645 1951 YKMA--VYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLF 1994
Cdd:cd04207    86 NPPWrdTVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 445-565 8.26e-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: 8.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  445 DETFKTRETIQHESGLLGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplharRLPR---GIKHVKDLPIHPGEIF 521
Cdd:cd13861    14 DLGGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL---------RLPNamdGVPGLTQPPVPPGESF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 569009645  522 KYKWTVtvedgPtksDPRclTRYYSSFINPERDLASGLIGPLLI 565
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 ...
 462-565 1.04e-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: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  462 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksdpr 539
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGL------FQNGTNwmDGTAGITQCPIPPGGSFTYNFTVDGQYG------- 96

                          90       100
                  ....*....|....*....|....*.
gi 569009645  540 clTRYYSSFINPErdLASGLIGPLLI 565
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 ...
 462-565 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: 43.06  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645  462 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksdpr 539
Cdd:cd13850    28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGI------LQRGTPwsDGVPGVTQWPIQPGGSFTYRWKAEDQYG------- 94

                          90       100
                  ....*....|....*....|....*.
gi 569009645  540 clTRYYSSFINPErdLASGLIGPLLI 565
Cdd:cd13850    95 --LYWYHSHYRGY--YMDGLYGPIYI 116
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 83-191 3.66e-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: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   83 GLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQtsqmekedDKVFPGESHTYVWQVlkengpmas 162
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGLTQ--------PPVPPGESFTYEFTP--------- 90

                          90       100
                  ....*....|....*....|....*....
gi 569009645  163 dPPCLTYSYMSHVDLVKDLNSGLIGALLV 191
Cdd:cd13861    91 -PDAGTYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 86-191 6.37e-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: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   86 GPTIWTEVHDTVVITLKNMASHPVSLHAVGVSywkaSEGDEYEDQT---SQMEkeddkVFPGESHTYVWQVLKENGpmas 162
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTagiTQCP-----IPPGGSFTYNFTVDGQYG---- 96

                          90       100
                  ....*....|....*....|....*....
gi 569009645  163 dppclTYSYMSHVDLvkDLNSGLIGALLV 191
Cdd:cd13857    97 -----TYWYHSHYST--QYADGLVGPLIV 118
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 433-532 8.99e-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: 8.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   433 RKYK-KVRFIAYTdETFKTRETIQHESGLLGPLLYGEVGDTLLIIFKNQASrpYNIYPHgitdvspLHARRLPR-----G 506
Cdd:TIGR03389    4 RHYTfDVQEKNVT-RLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQ--YNVTIH-------WHGVRQLRngwadG 73

                           90       100
                   ....*....|....*....|....*.
gi 569009645   507 IKHVKDLPIHPGEIFKYKWTVTVEDG 532
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 ...
 86-191 1.12e-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: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   86 GPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGdeyedqtSQMEKEDdkVFPGESHTYVWQVLK----ENGPMA 161
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDG-------TGMNASI--VAPGDTRIYTWRTHGgyrrADGSWA 99

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569009645  162 SDPPClTYSYMSHV----DLVKDLNSGLIGALLV 191
Cdd:cd14449   100 EGTAG-YWHYHDHVfgteHGTEGLSRGLYGALIV 132
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 460-565 2.63e-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: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   460 LLGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksd 537
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL------QQRGTPwmDGVPGVTQCPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 569009645   538 prclTRYYSSFINPERdlASGLIGPLLI 565
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 ...
 462-528 2.72e-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: 2.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569009645  462 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVSplharrlprgIKHVKDLPIHPGEIFKYKWTVT 528
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAA----------MDGTGLGPIMPGESFTYEFVAE 88
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 86-191 2.98e-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: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009645   86 GPTIWTEVHDTVVITLKN-MASHPVSLHAVGV----SYWkaSEGDEYEDQTSQMekeddkvfPGESHTYVWQVlkengpm 160
Cdd:cd13845    30 GPTIRATAGDTIVVELENkLPTEGVAIHWHGIrqrgTPW--ADGTASVSQCPIN--------PGETFTYQFVV------- 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 569009645  161 asDPPClTYSYMSHVDLVKdlNSGLIGALLV 191
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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