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Conserved domains on  [gi|569009643|ref|XP_006527852|]
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coagulation factor VIII isoform X1 [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 ...
 399-575 1.73e-105

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


:

Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 334.59  E-value: 1.73e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  399 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 478
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  479 TLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 558
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 569009643  559 ERDLASGLIGPLLICYK 575
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 22-202 3.92e-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: 313.45  E-value: 3.92e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   22 RRYYLGAVELSWNYIQSDLLSvlhtdsrfLPRMSTSFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVH 101
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGD--------PASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  102 DTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 181
Cdd:cd14452    73 DTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQ 152

                         170       180
                  ....*....|....*....|.
gi 569009643  182 VDLVKDLNSGLIGALLVCKEG 202
Cdd:cd14452   153 VDPVKDVNSGLIGALLVCRMG 173
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1684-1848 2.75e-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: 302.19  E-value: 2.75e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1684 TRHYFIAAVERLWDYGMSTS-HVLR----NRYQSDNVPQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDN 1758
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPqHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1759 IMVTFKNQASRPYSFYSSLISYKEDQRGeEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMHSGL 1838
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQRA-EPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGL 159

                         170
                  ....*....|
gi 569009643 1839 IGPLLICHAN 1848
Cdd:cd04228   160 IGPLIICKTG 169
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1860-2003 1.81e-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: 1.81e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1860 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1939
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009643 1940 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 2003
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 588-730 3.79e-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: 260.57  E-value: 3.79e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  588 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDF 667
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009643  668 LSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 730
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 212-346 1.89e-72

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


The actual alignment was detected with superfamily member cd11015:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 134  Bit Score: 238.27  E-value: 1.89e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  212 LYQFVLLFAVFDEGKSWHSETNDSYTQSmDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 291
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRD-KFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009643  292 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 346
Cdd:cd11015    80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2164-2310 1.03e-52

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: 182.17  E-value: 1.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 2164 PLGMESKvISDTQITASSYFTnmfATWSPSQARLHlqgRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSLFTSMF 2243
Cdd:cd00057     2 PLGMESG-LADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009643 2244 VKEFLISSSQDGHHWTQI--LYNGKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILG 2310
Cdd:cd00057    75 VTSYKVQYSLDGETWTTYkdKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2011-2155 1.31e-49

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


:

Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 173.31  E-value: 1.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 2011 PLGMASGsIRDFQITASGHYG-QWAPNLARLHysgSINAWSTKE--PFSWIKVDLLAPMIVHGIKTQGARQKFSSLYISQ 2087
Cdd:cd00057     2 PLGMESG-LADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009643 2088 FIIMYSLDGKKWLSYQGNstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMG 2155
Cdd:cd00057    78 YKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
rpoC2 super family cl33332
RNA polymerase beta'' subunit; Reviewed
 1134-1509 2.53e-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: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1134 NGNNSLNSEQEHSPKQLVYLMFKKYVKNQSFLSEKNKVTVEqdgFTKNIGLKdmafphnmSIFLTTLSNVHENGRHNQEK 1213
Cdd:CHL00117  741 PGTGKKNSKESKKIKNWIYVQRITPTKKKYFVLVRPVVTYE---IADGINLA--------TLFPQDLLQEKDNLQLRVVN 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1214 NIQEEIEKEalIEEkvvlpqvheaTGSKNFLKDILILGTRQ---NISLYEVH---VPVLQNitsiNNSTNTVQIHM--EH 1285
Cdd:CHL00117  810 YILYGNGKP--IRG----------ISSIQLVRTCLVLNWDQdkkSSSIEEARasfVEVRTN----GLIRDFLRINLvkSP 873

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1286 FFKRRKDKETNSEGLVNKTremvKNYPSQKNIttqrskraLGQFRLSTQWLKTincsTQCIIKQI-DHSKEMKKFITKSS 1364
Cdd:CHL00117  874 ISYIRKRNDPSSSGLLVQS----NNFLDSTNI--------YSKAEIQSQSLSQ----NQGTIRTLlNRNKESQSLLILSS 937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1365 lSDSSVIKSTTQTNSSDSHIVKTSAFPPIDLKRSPFQNKFSHVQASSYIYDFKTKSSRIqesNNFLKETKINNPSLAILP 1444
Cdd:CHL00117  938 -SDCFRIGPFNGKKSKYHNIKESNPLIPIRNSLGPLGTVLQIANFSSSYHLLTHNQILV---TKYLQLDNLKQTFQVKVL 1013

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009643 1445 WNMFIDQ-GKFTSPgKSNTNSVTYKKRENIIFLKPTLPEESGKIELLPQvSIQEEEILPTETSHGS 1509
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 ...
 399-575 1.73e-105

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 334.59  E-value: 1.73e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  399 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 478
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  479 TLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 558
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 569009643  559 ERDLASGLIGPLLICYK 575
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-202 3.92e-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: 313.45  E-value: 3.92e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   22 RRYYLGAVELSWNYIQSDLLSvlhtdsrfLPRMSTSFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVH 101
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGD--------PASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  102 DTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 181
Cdd:cd14452    73 DTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQ 152

                         170       180
                  ....*....|....*....|.
gi 569009643  182 VDLVKDLNSGLIGALLVCKEG 202
Cdd:cd14452   153 VDPVKDVNSGLIGALLVCRMG 173
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1684-1848 2.75e-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: 302.19  E-value: 2.75e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1684 TRHYFIAAVERLWDYGMSTS-HVLR----NRYQSDNVPQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDN 1758
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPqHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1759 IMVTFKNQASRPYSFYSSLISYKEDQRGeEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMHSGL 1838
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQRA-EPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGL 159

                         170
                  ....*....|
gi 569009643 1839 IGPLLICHAN 1848
Cdd:cd04228   160 IGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1860-2003 1.81e-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: 1.81e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1860 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1939
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009643 1940 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 2003
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 588-730 3.79e-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: 260.57  E-value: 3.79e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  588 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDF 667
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009643  668 LSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 730
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 212-346 1.89e-72

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 238.27  E-value: 1.89e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  212 LYQFVLLFAVFDEGKSWHSETNDSYTQSmDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 291
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRD-KFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009643  292 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 346
Cdd:cd11015    80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2164-2310 1.03e-52

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: 182.17  E-value: 1.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 2164 PLGMESKvISDTQITASSYFTnmfATWSPSQARLHlqgRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSLFTSMF 2243
Cdd:cd00057     2 PLGMESG-LADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009643 2244 VKEFLISSSQDGHHWTQI--LYNGKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILG 2310
Cdd:cd00057    75 VTSYKVQYSLDGETWTTYkdKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2011-2155 1.31e-49

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


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 173.31  E-value: 1.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 2011 PLGMASGsIRDFQITASGHYG-QWAPNLARLHysgSINAWSTKE--PFSWIKVDLLAPMIVHGIKTQGARQKFSSLYISQ 2087
Cdd:cd00057     2 PLGMESG-LADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009643 2088 FIIMYSLDGKKWLSYQGNstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMG 2155
Cdd:cd00057    78 YKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2008-2156 4.37e-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: 4.37e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   2008 CQIPLGMASgsirDFQITASGHYgqWAPNLARLHYsGSINAWSTKEP--FSWIKVDLLAPMIVHGIKTQGArqkFSSLYI 2085
Cdd:smart00231    2 CNEPLGLES----DSQITASSSY--WAAKIARLNG-GSDGGWCPAKNdlPPWIQVDLGRLRTVTGVITGRR---HGNGDW 71

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009643   2086 SQFIIMYSLDGKKWLSYQGnstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMGC 2156
Cdd:smart00231   72 VTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2160-2311 1.29e-32

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: 124.54  E-value: 1.29e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   2160 SCSIPLGMESkvisDTQITASSyftnmfATWSPSQARLHlQGRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlf 2239
Cdd:smart00231    1 PCNEPLGLES----DSQITASS------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHG-- 67

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009643   2240 TSMFVKEFLISSSqDGHHWTQI-LYNGKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILGC 2311
Cdd:smart00231   68 NGDWVTYKLEYSD-DGVNWTTYkDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2176-2308 6.75e-30

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


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 116.01  E-value: 6.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  2176 QITASSYFTNmfaTWsPSQARLHLQGRTnAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlFTSMFVKEFLISSSQDG 2255
Cdd:pfam00754    1 QITASSSYSG---EG-PAAAALDGDPNT-AWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 569009643  2256 HHWTQILYNGkvFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIW--EHQIALRLEI 2308
Cdd:pfam00754   75 ENWTTVKDEK--IPGNNDNNTPVTNTFDPPIKARYVRIVPTSWngGNGIALRAEL 127
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2023-2153 2.64e-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: 105.99  E-value: 2.64e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  2023 QITASGHY-GQWAPNlARLHysGSIN-AWSTKE--PFSWIKVDLLAPMIVHGIKTQGaRQKFSSLYISQFIIMYSLDGKK 2098
Cdd:pfam00754    1 QITASSSYsGEGPAA-AALD--GDPNtAWSAWSgdDPQWIQVDLGKPKKITGVVTQG-RQDGSNGYVTSYKIEYSLDGEN 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009643  2099 WLSYQGNSTgtlmvfFGNVDSSGIKHNSFNPPIIARYIRLHPT--HSSIRSTLRMEL 2153
Cdd:pfam00754   77 WTTVKDEKI------PGNNDNNTPVTNTFDPPIKARYVRIVPTswNGGNGIALRAEL 127
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 219-350 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 569009643   219 FAVFDEGKSWHSETNDSYTQSMDsASARDWPKM------HTVNGYVNRSLPGLIGCHRKSVYWHVIgMGTTPEIHSIFLE 292
Cdd:pfam00394    1 EDYVITLSDWYHKDAKDLEKELL-ASGKAPTDFppvpdaVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009643   293 GHTF--------FVRNHRQASLEISPITFLTAQ-TLLIDLGQFLLFCH-ISSHKHDGMEAYVKVDSCP 350
Cdd:pfam00394   79 GHKMtvvevdgvYVNPFTVDSLDIFPGQRYSVLvTANQDPGNYWIVASpNIPAFDNGTAAAILRYSGA 146
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1884-2007 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 569009643  1884 RNCKTPCNFQMEDPTLkeNYRFHAINGYVMD-TLPGLVMAQDQRIRWYLLsmgNNENI-QSIHFSGHVFTV-----RKKE 1956
Cdd:pfam07731    2 TPPKLPTLLQITSGNF--RRNDWAINGLLFPpNTNVITLPYGTVVEWVLQ---NTTTGvHPFHLHGHSFQVlgrggGPWP 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009643  1957 EYKMAVYNL-----------YPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVYSKQ 2007
Cdd:pfam07731   77 EEDPKTYNLvdpvrrdtvqvPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
rpoC2 CHL00117
RNA polymerase beta'' subunit; Reviewed
 1134-1509 2.53e-05

RNA polymerase beta'' subunit; Reviewed


Pssm-ID: 214368 [Multi-domain]  Cd Length: 1364  Bit Score: 49.94  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1134 NGNNSLNSEQEHSPKQLVYLMFKKYVKNQSFLSEKNKVTVEqdgFTKNIGLKdmafphnmSIFLTTLSNVHENGRHNQEK 1213
Cdd:CHL00117  741 PGTGKKNSKESKKIKNWIYVQRITPTKKKYFVLVRPVVTYE---IADGINLA--------TLFPQDLLQEKDNLQLRVVN 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1214 NIQEEIEKEalIEEkvvlpqvheaTGSKNFLKDILILGTRQ---NISLYEVH---VPVLQNitsiNNSTNTVQIHM--EH 1285
Cdd:CHL00117  810 YILYGNGKP--IRG----------ISSIQLVRTCLVLNWDQdkkSSSIEEARasfVEVRTN----GLIRDFLRINLvkSP 873

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1286 FFKRRKDKETNSEGLVNKTremvKNYPSQKNIttqrskraLGQFRLSTQWLKTincsTQCIIKQI-DHSKEMKKFITKSS 1364
Cdd:CHL00117  874 ISYIRKRNDPSSSGLLVQS----NNFLDSTNI--------YSKAEIQSQSLSQ----NQGTIRTLlNRNKESQSLLILSS 937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1365 lSDSSVIKSTTQTNSSDSHIVKTSAFPPIDLKRSPFQNKFSHVQASSYIYDFKTKSSRIqesNNFLKETKINNPSLAILP 1444
Cdd:CHL00117  938 -SDCFRIGPFNGKKSKYHNIKESNPLIPIRNSLGPLGTVLQIANFSSSYHLLTHNQILV---TKYLQLDNLKQTFQVKVL 1013

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009643 1445 WNMFIDQ-GKFTSPgKSNTNSVTYKKRENIIFLKPTLPEESGKIELLPQvSIQEEEILPTETSHGS 1509
Cdd:CHL00117 1014 KYYLIDEnGKIYNP-DPCSNIILNPFNLNWYFLHHNYCEETSTIISLGQ-FICENVCISKNGPHKS 1077
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 440-539 9.01e-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: 9.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   440 RKYK-KVRFIAYTdETFKTRETIQHESGLLGPLLYGEVGDTLLIIFKNQASrpYNIYPHgitdvspLHARRLPR-----G 513
Cdd:TIGR03389    4 RHYTfDVQEKNVT-RLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQ--YNVTIH-------WHGVRQLRngwadG 73

                           90       100
                   ....*....|....*....|....*.
gi 569009643   514 IKHVKDLPIHPGEIFKYKWTVTVEDG 539
Cdd:TIGR03389   74 PAYITQCPIQPGQSYVYNFTITGQRG 99
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 467-572 2.37e-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: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   467 LLGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksd 544
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL------QQRGTPwmDGVPGVTQCPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 569009643   545 prclTRYYSSFINPERdlASGLIGPLLI 572
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 ...
 399-575 1.73e-105

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 334.59  E-value: 1.73e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  399 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 478
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  479 TLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 558
Cdd:cd04227    81 QIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDP 160

                         170
                  ....*....|....*..
gi 569009643  559 ERDLASGLIGPLLICYK 575
Cdd:cd04227   161 ERDLASGLIGPLLICKK 177
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 22-202 3.92e-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: 313.45  E-value: 3.92e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   22 RRYYLGAVELSWNYIQSDLLSvlhtdsrfLPRMSTSFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVH 101
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDLGD--------PASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  102 DTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 181
Cdd:cd14452    73 DTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQ 152

                         170       180
                  ....*....|....*....|.
gi 569009643  182 VDLVKDLNSGLIGALLVCKEG 202
Cdd:cd14452   153 VDPVKDVNSGLIGALLVCRMG 173
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1684-1848 2.75e-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: 302.19  E-value: 2.75e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1684 TRHYFIAAVERLWDYGMSTS-HVLR----NRYQSDNVPQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDN 1758
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPqHFLRardpNRGRRKSVPQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1759 IMVTFKNQASRPYSFYSSLISYKEDQRGeEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMHSGL 1838
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEEDQRA-EPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGL 159

                         170
                  ....*....|
gi 569009643 1839 IGPLLICHAN 1848
Cdd:cd04228   160 IGPLIICKTG 169
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1860-2003 1.81e-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: 1.81e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1860 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1939
Cdd:cd11018     1 VQEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009643 1940 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 2003
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 ...
 22-201 1.18e-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: 271.97  E-value: 1.18e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   22 RRYYLGAVELSWNYIQSDLLsvlHTDSRFLPRMSTSFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVH 101
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLA---EKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAEVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  102 DTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 181
Cdd:cd04199    78 DTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSH 157

                         170       180
                  ....*....|....*....|
gi 569009643  182 VDLVKDLNSGLIGALLVCKE 201
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 ...
 401-575 7.34e-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: 269.66  E-value: 7.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  401 WIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGDTL 480
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAEVGDTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  481 LIIFKNQASRPYNIYPHGITDVSPLHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINP 558
Cdd:cd04199    81 KVHFKNKASRPYSIHPHGVSYEKDSEGASYSdqTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHVDL 160

                         170
                  ....*....|....*..
gi 569009643  559 ERDLASGLIGPLLICYK 575
Cdd:cd04199   161 EKDINSGLIGPLLICKK 177
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 588-730 3.79e-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: 260.57  E-value: 3.79e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  588 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDF 667
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009643  668 LSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 730
Cdd:cd11016    81 LSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 1685-1847 1.67e-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: 240.00  E-value: 1.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1685 RHYFIAAVERLWDYGMSTSH--------VLRNRYQSDNVPQFKKVVFQEFTDGSFSQPlyrGELNEHLGLLGPYIRAEVE 1756
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAekdlsyrnQYLDNGPFRIGRSYKKVVYREYTDESFTTP---GPQPEHLGILGPTIRAEVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1757 DNIMVTFKNQASRPYSFYSSLISYKEDQRG---------EEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSD 1827
Cdd:cd04199    78 DTIKVHFKNKASRPYSIHPHGVSYEKDSEGasysdqtgpDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSH 157

                         170       180
                  ....*....|....*....|
gi 569009643 1828 VDLERDMHSGLIGPLLICHA 1847
Cdd:cd04199   158 VDLEKDINSGLIGPLLICKK 177
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 212-346 1.89e-72

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 238.27  E-value: 1.89e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  212 LYQFVLLFAVFDEGKSWHSETNDSYTQSmDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 291
Cdd:cd11015     1 NQAFVLLFAVFDEGKSWYSEVGERKSRD-KFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009643  292 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 346
Cdd:cd11015    80 EGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 399-573 4.19e-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: 216.28  E-value: 4.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  399 KTWIHYISAEEEDWDYAPSVPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQH--ESGLLGPLLYGEV 476
Cdd:cd14450     1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRpkEEGILGPVIRAQV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  477 GDTLLIIFKNQASRPYNIYPHGITdVSP-----LHARRLPRGIKHVKdlPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRY 551
Cdd:cd14450    81 RDTIKIVFKNKASRPYSIYPHGVT-VSKaaegaSYPPDPRGNETQNK--AVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                         170       180
                  ....*....|....*....|..
gi 569009643  552 YSSFINPERDLASGLIGPLLIC 573
Cdd:cd14450   158 YHSAVDITRDIASGLIGPLLIC 179
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 1860-2003 3.33e-63

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 211.88  E-value: 3.33e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1860 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1939
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009643 1940 IQSIHFSGHVFTVRKkeeYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 2003
Cdd:cd04200    81 VHSIHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 588-727 3.08e-60

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 203.41  E-value: 3.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  588 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTD 666
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPgLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009643  667 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 727
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 ...
 22-202 9.59e-60

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: 203.17  E-value: 9.59e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   22 RRYYLGAVELSWNYI-QSDLLSVLHTDSrflprmstsfpfntsiMYKKTVFVEYKDQlFNIAKPRPPWMGLLGPTIWTEV 100
Cdd:cd04226     1 REYYIAAQNIDWDYTpQSEELRLKRSEQ----------------SFKKIVYREYEEG-FKKEKPADLSSGLLGPTLRAEV 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  101 HDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMS 180
Cdd:cd04226    64 GDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYS 143

                         170       180
                  ....*....|....*....|..
gi 569009643  181 HVDLVKDLNSGLIGALLVCKEG 202
Cdd:cd04226   144 HVNMVRDFNSGLIGALLICKKG 165
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-201 1.05e-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: 192.25  E-value: 1.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   22 RRYYLGAVELSWNYIQS--DLLSVLHTDSRflpRMSTSF----PFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPT 95
Cdd:cd04222     1 REYYIGIRETQWDYAPSgkNLITNQTFDDD---EHASVFlkrgPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   96 IWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLT 175
Cdd:cd04222    78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                         170       180
                  ....*....|....*....|....*.
gi 569009643  176 YSYMSHVDLVKDLNSGLIGALLVCKE 201
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 ...
 1684-1845 2.39e-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: 190.82  E-value: 2.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1684 TRHYFIAAVERLWDY-GMSTSHVLRNRYQSDNVpqFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPYIRAEVEDNIMVT 1762
Cdd:cd14451     1 KRRYYIAAEEEEWDYaGYGKSRLDKTQNERDTV--FKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1763 FKNQASRPYSFYSSLISYKEDQRG-----EEP----RRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERD 1833
Cdd:cd14451    79 FKNLASRPYSLHAHGLSYEKSSEGlsyddESPdwfkKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKD 158

                         170
                  ....*....|..
gi 569009643 1834 MHSGLIGPLLIC 1845
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 ...
 214-346 9.71e-55

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 187.62  E-value: 9.71e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  214 QFVLLFAVFDEGKSWHSETNDSYTQS------MDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 287
Cdd:cd04200     3 EFVLLFAVFDENKSWYLEDNIKRFCDnpekvdKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569009643  288 SIFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 346
Cdd:cd04200    83 SIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2164-2310 1.03e-52

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: 182.17  E-value: 1.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 2164 PLGMESKvISDTQITASSYFTnmfATWSPSQARLHlqgRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSLFTSMF 2243
Cdd:cd00057     2 PLGMESG-LADDQITASSSYS---SGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569009643 2244 VKEFLISSSQDGHHWTQI--LYNGKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILG 2310
Cdd:cd00057    75 VTSYKVQYSLDGETWTTYkdKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 403-584 3.30e-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: 3.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  403 HYISAEEEDWDYAPS-------VPTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHES---GLLGPLL 472
Cdd:cd04224     6 YFIAAEEIMWDYAPSgknlftgQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEehlGILGPVI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  473 YGEVGDTLLIIFKNQASRPYNIYPHGI-----TDVSPLHARRLPRGikhvkdLPIHPGEIFKYKWTVTVEDGPTKSDPRC 547
Cdd:cd04224    86 RAEVGDTIKVTFRNKASRPFSIQPHGVfyeknYEGAMYRDGDPSPG------SHVSPGETFTYEWTVPEGVGPTNQDPPC 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 569009643  548 LTRYYSSFINPERDLASGLIGPLLICYKESVDQRGNQ 584
Cdd:cd04224   160 LTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQ 196
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2011-2155 1.31e-49

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


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 173.31  E-value: 1.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 2011 PLGMASGsIRDFQITASGHYG-QWAPNLARLHysgSINAWSTKE--PFSWIKVDLLAPMIVHGIKTQGARQKFSSLYISQ 2087
Cdd:cd00057     2 PLGMESG-LADDQITASSSYSsGWEASRARLN---SDNAWTPAVndPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009643 2088 FIIMYSLDGKKWLSYQGNstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMG 2155
Cdd:cd00057    78 YKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1683-1858 7.63e-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: 7.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1683 KTRHYFIAAVERLWDYGMS----TSHVLRNRYQSDNVP-----------QFKKVVFQEFTDGSFSQPLYRGELNEHLGLL 1747
Cdd:cd04224     2 KVRHYFIAAEEIMWDYAPSgknlFTGQNLTAPGSDSEVffqrnetriggTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1748 GPYIRAEVEDNIMVTFKNQASRPYSFYSSLISYKEDQRGEEPRRNF------VKPNETKIYFWKVQHHMAPTEDEFDCKA 1821
Cdd:cd04224    82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDpspgshVSPGETFTYEWTVPEGVGPTNQDPPCLT 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 569009643 1822 WAYFSDVDLERDMHSGLIGPLLICHANTLNpAHGRQV 1858
Cdd:cd04224   162 YLYFSAVDPVRDTNSGLVGPLLVCKKGSLN-ANGRQK 197
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 402-575 1.23e-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: 1.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  402 IHYISAEEEDWDYAPSV------PTSDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFktRETIQHES--GLLGPLLY 473
Cdd:cd04222     2 EYYIGIRETQWDYAPSGknlitnQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTY--RTEIEKPVwlGFLGPILK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  474 GEVGDTLLIIFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHV--KDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRY 551
Cdd:cd04222    80 AEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFekADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRI 159

                         170       180
                  ....*....|....*....|....
gi 569009643  552 YSSFINPERDLASGLIGPLLICYK 575
Cdd:cd04222   160 YHSHIDAPKDIASGLIGPLIICKK 183
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 21-210 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 569009643   21 IRRYYLGAVELSWNYIQSDLLSVLHTDSRflPRMSTSFPF----NTSI--MYKKTVFVEYKDQLFNIAKPRPP---WMGL 91
Cdd:cd04224     3 VRHYFIAAEEIMWDYAPSGKNLFTGQNLT--APGSDSEVFfqrnETRIggTYWKVRYVEYTDATFTTRKHRSKeeeHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   92 LGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTsqmEKEDDKVFPGESHTYVWQVLKENGPMASDP 171
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGD---PSPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 569009643  172 PCLTYSYMSHVDLVKDLNSGLIGALLVCKEGSLSKERTQ 210
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 ...
 22-202 5.06e-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: 166.94  E-value: 5.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   22 RRYYLGAVELSWNY---IQSDLlsvlhtdsrflprMSTSFPFNTSimYKKTVFVEYKDQLFNIAKPRPPW---MGLLGPT 95
Cdd:cd14451     2 RRYYIAAEEEEWDYagyGKSRL-------------DKTQNERDTV--FKKVVFRRYLDSTFSTPDIQGEYeehLGILGPV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   96 IWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLT 175
Cdd:cd14451    67 IRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRT 146

                         170       180
                  ....*....|....*....|....*..
gi 569009643  176 YSYMSHVDLVKDLNSGLIGALLVCKEG 202
Cdd:cd14451   147 WAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 402-575 6.21e-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: 158.01  E-value: 6.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  402 IHYISAEEEDWDYAPSVPTSD------NGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETF---KTRETIQHESGLLGPLL 472
Cdd:cd04225     2 TYYIAAEEVEWDYSPQRTWEQelhnthEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFsvpKERTAEEEHLGILGPLI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  473 YGEVGDTLLIIFKNQASRPYNIYPHGITDVSPLHArrlprgikhvkdlPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYY 552
Cdd:cd04225    82 HAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVA-------------PTEPGETQTYTWKIPERSGPGVEDSNCISWAY 148

                         170       180
                  ....*....|....*....|...
gi 569009643  553 SSFINPERDLASGLIGPLLICYK 575
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 ...
 24-200 1.02e-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: 1.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   24 YYLGAVELSWNYIQSdllSVLHTDSRFLPRMSTSFPFNTSIMYKKTVFVEYKDQLFN--IAKPRPPWMGLLGPTIWTEVH 101
Cdd:cd14450     5 YFIAAEEVIWDYAPS---IPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTkrLENPRPKEEGILGPVIRAQVR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  102 DTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQTSQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 181
Cdd:cd14450    82 DTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHSA 161

                         170
                  ....*....|....*....
gi 569009643  182 VDLVKDLNSGLIGALLVCK 200
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 ...
 1687-1845 2.89e-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: 148.10  E-value: 2.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1687 YFIAAVERLWDYGMSTSHVLRNRYQS---DNVPQF-----KKVVFQEFTDGSFSQPLYRGELNEhLGLLGPYIRAEVEDN 1758
Cdd:cd14450     5 YFIAAEEVIWDYAPSIPENMDKRYRSqylDNFSNNigkkyKKAVFTQYEDGSFTKRLENPRPKE-EGILGPVIRAQVRDT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1759 IMVTFKNQASRPYSFYSSLISYKEDQRG----EEPRRNF-----VKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVD 1829
Cdd:cd14450    84 IKIVFKNKASRPYSIYPHGVTVSKAAEGasypPDPRGNEtqnkaVQPGETYTYKWNILETDEPTARDPRCLTRMYHSAVD 163

                         170
                  ....*....|....*.
gi 569009643 1830 LERDMHSGLIGPLLIC 1845
Cdd:cd14450   164 ITRDIASGLIGPLLIC 179
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1685-1845 3.95e-40

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 147.23  E-value: 3.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1685 RHYFIAAVERLWDYGMSTS-----HVLRNRYQSDNV---------PQFKKVVFQEFTDGSFSQPLYRGELNEHLGLLGPY 1750
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTweqelHNTHEESPGNAFlnkgdkfigSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1751 IRAEVEDNIMVTFKNQASRPYSFYSSLIsyKEDQrgeePRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDL 1830
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGV--KTDS----SWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQ 154

                         170
                  ....*....|....*
gi 569009643 1831 ERDMHSGLIGPLLIC 1845
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 ...
 1860-2003 5.01e-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: 5.01e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1860 VQEFALLFTIFDETKSWYFTENVKRNCKtpcNFQMEDPTLKENYRFHAINGYVMDtLPGLVMAQDQRIRWYLLSMGNNEN 1939
Cdd:cd14455     1 RREFVLLFMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKD 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009643 1940 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 2003
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 ...
 588-721 7.97e-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: 7.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  588 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTD 666
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSApLGFCHSEVVQWHISSVGTQDE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009643  667 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGM 721
Cdd:cd14454    81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGL 135
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1860-2003 1.31e-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: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1860 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1939
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009643 1940 IQSIHFSGHVFTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 2003
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 403-572 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 569009643  403 HYISAEEEDWDYAPSVPT----SDNGSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGD 478
Cdd:cd04229     3 YYIAAEEVDWDYAPSGKNkcclGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRAEVGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  479 TLLIIFKNQASR-PYNIYPHGITdVSPLHARRLPRGIKHVKdlpihPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFIN 557
Cdd:cd04229    83 TIKVVFKNNLDEfPVNMHPHGGL-YSKDNEGTTDGAGDVVA-----PGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHVD 156

                         170
                  ....*....|....*
gi 569009643  558 PERDLASGLIGPLLI 572
Cdd:cd04229   157 VFAHTNAGLVGPIIV 171
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2008-2156 4.37e-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: 4.37e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   2008 CQIPLGMASgsirDFQITASGHYgqWAPNLARLHYsGSINAWSTKEP--FSWIKVDLLAPMIVHGIKTQGArqkFSSLYI 2085
Cdd:smart00231    2 CNEPLGLES----DSQITASSSY--WAAKIARLNG-GSDGGWCPAKNdlPPWIQVDLGRLRTVTGVITGRR---HGNGDW 71

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009643   2086 SQFIIMYSLDGKKWLSYQGnstGTLMVFFGNVDSSGIKHNSFNPPIIARYIRLHPTHSSIRSTLRMELMGC 2156
Cdd:smart00231   72 VTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 403-575 8.95e-38

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: 8.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  403 HYISAEEEDWDYAPSVPTSDNGSYKSQYLSngphrigrkYKKVRFIAYTDETFKTRET---IQHESGLLGPLLYGEVGDT 479
Cdd:cd14451     4 YYIAAEEEEWDYAGYGKSRLDKTQNERDTV---------FKKVVFRRYLDSTFSTPDIqgeYEEHLGILGPVIRAEVDDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  480 LLIIFKNQASRPYNIYPHGITDVSPLHARRL----PRGIKhvKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSF 555
Cdd:cd14451    75 IQVFFKNLASRPYSLHAHGLSYEKSSEGLSYddesPDWFK--KDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSA 152

                         170       180
                  ....*....|....*....|
gi 569009643  556 INPERDLASGLIGPLLICYK 575
Cdd:cd14451   153 VNPEKDIHSGLIGPLLICRK 172
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1860-2003 1.31e-37

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 138.76  E-value: 1.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1860 VQEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNEN 1939
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009643 1940 IQSIHFSGHVFTVRKkeeYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 2003
Cdd:cd11021    81 IHSAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 403-575 1.42e-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: 1.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  403 HYISAEEEDWDYAPsvptsdngsyksQYLSNGPHRIGRKYKKVRFIAYtDETFKTRETIQHESGLLGPLLYGEVGDTLLI 482
Cdd:cd04226     3 YYIAAQNIDWDYTP------------QSEELRLKRSEQSFKKIVYREY-EEGFKKEKPADLSSGLLGPTLRAEVGDTLIV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  483 IFKNQASRPYNIYPHGITDVSPLHARRLPRGIKHVK--DLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINPER 560
Cdd:cd04226    70 HFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEklDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVR 149

                         170
                  ....*....|....*
gi 569009643  561 DLASGLIGPLLICYK 575
Cdd:cd04226   150 DFNSGLIGALLICKK 164
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 22-202 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 569009643   22 RRYYLGAVELSWNYIQSDLLSVLHTD--SRFLPRMSTSfPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTE 99
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKNKCCLGDdlEVSTLDSQPG-PYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  100 VHDTVVITLKN-MASHPVSLHAVGVSYWKASEGdeyedqtsQMEKEDDKVFPGESHTYVWQVLKENGPMASDPPCLTYSY 178
Cdd:cd04229    80 VGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEG--------TTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLY 151

                         170       180
                  ....*....|....*....|....
gi 569009643  179 MSHVDLVKDLNSGLIGALLVCKEG 202
Cdd:cd04229   152 HSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 588-727 8.10e-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: 136.45  E-value: 8.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  588 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSL-ELTVCLHEVAYWHILSVGAQTD 666
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLpGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009643  667 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 727
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 588-730 1.97e-36

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 135.30  E-value: 1.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  588 DKRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTD 666
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPgLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569009643  667 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKVSSC 730
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1685-1845 2.66e-36

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 136.78  E-value: 2.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1685 RHYFIAAVERLWDYGMSTSHVLRNR-YQSD--------NVPQ-----FKKVVFQEFTDGSFSQPLyrgELNEHLGLLGPY 1750
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQtFDDDehasvflkRGPDrigrvYKKAVYLQYTDDTYRTEI---EKPVWLGFLGPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1751 IRAEVEDNIMVTFKNQASRPYSFYSSLISYKEDQRGE---------EPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKA 1821
Cdd:cd04222    78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGAlypdntsgfEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                         170       180
                  ....*....|....*....|....
gi 569009643 1822 WAYFSDVDLERDMHSGLIGPLLIC 1845
Cdd:cd04222   158 RIYHSHIDAPKDIASGLIGPLIIC 181
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1685-1845 1.85e-34

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 130.87  E-value: 1.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1685 RHYFIAAVERLWDYGMST--SHVLRNRYQSDNVPQ-FKKVVFQEFTDGSFSQPLYRGELnehLGLLGPYIRAEVEDNIMV 1761
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSDlgDPASEQRKKPKDIPQkYIKAVFVEYLDATFTVPKPRPAW---MGLLGPTIVAEVGDTVVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1762 TFKNQASRPYSFYSSLISY--------KEDQ-RGEEPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLER 1832
Cdd:cd14452    78 TFKNLASQPYSLHAVGVSYwkasegagYDDStSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVK 157

                         170
                  ....*....|...
gi 569009643 1833 DMHSGLIGPLLIC 1845
Cdd:cd14452   158 DVNSGLIGALLVC 170
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1861-2008 3.62e-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: 3.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1861 QEFALLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1940
Cdd:cd11022     2 KEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009643 1941 QSIHFSGHvfTVRKKEEYKMAVyNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVysKQC 2008
Cdd:cd11022    82 HGIYFSGN--TFLLQGTRRDTA-NLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV--SQC 144
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 22-200 4.17e-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: 129.89  E-value: 4.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   22 RRYYLGAVELSWNYIQS----DLLSVLHTDSRFLPRMSTSFPFNTSiMYKKTVFVEYKDQLFNIAKPRPPWM---GLLGP 94
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQrtweQELHNTHEESPGNAFLNKGDKFIGS-KYKKVVYREYTDDTFSVPKERTAEEehlGILGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   95 TIWTEVHDTVVITLKNMASHPVSLHAVGVSywkasegdeyEDQTSQMEKEddkvfPGESHTYVWQVLKENGPMASDPPCL 174
Cdd:cd04225    80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVK----------TDSSWVAPTE-----PGETQTYTWKIPERSGPGVEDSNCI 144

                         170       180
                  ....*....|....*....|....*.
gi 569009643  175 TYSYMSHVDLVKDLNSGLIGALLVCK 200
Cdd:cd04225   145 SWAYYSTVDQIKDLYSGLIGPLVICR 170
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 21-202 4.95e-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: 129.62  E-value: 4.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   21 IRRYYLGAVELSWNYIQSDLLSVLHtdSRFLPR-MSTSFPfntsiMYKKTVFVEYKDQLFNIAKPR---PPWMGLLGPTI 96
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPQHFLR--ARDPNRgRRKSVP-----QYKKVVFREYLDGSFTQPVYRgelDEHLGILGPYI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   97 WTEVHDTVVITLKNMASHPVSLHAVGVSYwkasegdeYEDQTSQMEKEddKVFPGESHTYVWQVLKENGPMASDPPCLTY 176
Cdd:cd04228    74 RAEVEDNIMVTFKNLASRPYSFHSSLISY--------EEDQRAEPRGN--FVQPGEVQTYSWKVLHQMAPTKQEFDCKAW 143

                         170       180
                  ....*....|....*....|....*.
gi 569009643  177 SYMSHVDLVKDLNSGLIGALLVCKEG 202
Cdd:cd04228   144 AYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 403-573 6.12e-34

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 129.33  E-value: 6.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  403 HYISAEEEDWDYApsvpTSDNGSYKSQYLSNgPHRIGRKYKKVRFIAYTDETFKTRETIQHESGLLGPLLYGEVGDTLLI 482
Cdd:cd14452     3 YYIAAVEIGWDYI----HSDLGDPASEQRKK-PKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGDTVVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  483 IFKNQASRPYNIYPHGIT-----------DVSPLHARrlprgikhvKDLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRY 551
Cdd:cd14452    78 TFKNLASQPYSLHAVGVSywkasegagydDSTSQHEK---------EDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYS 148

                         170       180
                  ....*....|....*....|..
gi 569009643  552 YSSFINPERDLASGLIGPLLIC 573
Cdd:cd14452   149 YSSQVDPVKDVNSGLIGALLVC 170
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 403-573 7.28e-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: 7.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  403 HYISAEEEDWDYAPSVPTSdngSYKSQYLSNGPHRIGRKYKKVRFIAYTDETFK---TRETIQHESGLLGPLLYGEVGDT 479
Cdd:cd04228     4 YFIAAVEVLWDYGMQRPQH---FLRARDPNRGRRKSVPQYKKVVFREYLDGSFTqpvYRGELDEHLGILGPYIRAEVEDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  480 LLIIFKNQASRPYNIYPHGITDVSplHARRLPRGikhvkdLPIHPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFINPE 559
Cdd:cd04228    81 IMVTFKNLASRPYSFHSSLISYEE--DQRAEPRG------NFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLE 152

                         170
                  ....*....|....
gi 569009643  560 RDLASGLIGPLLIC 573
Cdd:cd04228   153 KDLHSGLIGPLIIC 166
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2160-2311 1.29e-32

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: 124.54  E-value: 1.29e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   2160 SCSIPLGMESkvisDTQITASSyftnmfATWSPSQARLHlQGRTNAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlf 2239
Cdd:smart00231    1 PCNEPLGLES----DSQITASS------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHG-- 67

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009643   2240 TSMFVKEFLISSSqDGHHWTQI-LYNGKVFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIWEHQIALRLEILGC 2311
Cdd:smart00231   68 NGDWVTYKLEYSD-DGVNWTTYkDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 24-200 2.38e-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: 2.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   24 YYLGAVELSWNYiqSDLLSVlHTDSRFLPRMSTSFPFNTSIMYKKTVFVEYKDQLFNIAKPRPPWMGLLGPTIWTEVHDT 103
Cdd:cd04227     5 HYIAAEELDWDY--APLLSS-TDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGDQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  104 VVITLKNMASHPVSLHAVGVSywkaSEGDEYEDQTSQMEKE--DDKVFPGESHTYVWQVLKENGPMASDPPCLTYSYMSH 181
Cdd:cd04227    82 IHIMFKNTASRPYNIYPHGLT----SVRPMYRSRNPAGEKDlkTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQST 157

                         170
                  ....*....|....*....
gi 569009643  182 VDLVKDLNSGLIGALLVCK 200
Cdd:cd04227   158 VDPERDLASGLIGPLLICK 176
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1683-1845 2.70e-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: 2.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1683 KTRHYFIAAVERLWDYGMSTSHVLRNRYQS---DNVPQ-----FKKVVFQEFTDGSFSQplyRGELNEHLGLLGPYIRAE 1754
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSrylPTGPQrigykYKKVAFVEYTDKTFKR---REAKQTEKGILGPLLKGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1755 VEDNIMVTFKNQASRPYSFY----SSLISYK--EDQRGEEPRRNF-VKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSD 1827
Cdd:cd04227    78 VGDQIHIMFKNTASRPYNIYphglTSVRPMYrsRNPAGEKDLKTMpIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQST 157

                         170
                  ....*....|....*...
gi 569009643 1828 VDLERDMHSGLIGPLLIC 1845
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 ...
 1685-1845 3.75e-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: 3.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1685 RHYFIAAVERLWDYGMSTSHVLRNRYQsdnvPQFKKVVFQEFTDGsFSQPLYRGELNehlGLLGPYIRAEVEDNIMVTFK 1764
Cdd:cd04226     1 REYYIAAQNIDWDYTPQSEELRLKRSE----QSFKKIVYREYEEG-FKKEKPADLSS---GLLGPTLRAEVGDTLIVHFK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1765 NQASRPYSFYSSLISYKEDQRGE---------EPRRNFVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDLERDMH 1835
Cdd:cd04226    73 NMADKPLSIHPQGIAYGKKSEGSlysdntspvEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFN 152

                         170
                  ....*....|
gi 569009643 1836 SGLIGPLLIC 1845
Cdd:cd04226   153 SGLIGALLIC 162
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1685-1844 6.21e-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: 6.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1685 RHYFIAAVERLWDYGMSTS---HVLRNRYQSDNVPQ---------FKKVVFQEFTDGSFSQPLyrgELNEHLGLLGPYIR 1752
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKnkcCLGDDLEVSTLDSQpgpytigstYTKARYREYTDNSFSTPK---PTPAYLGILGPVIR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1753 AEVEDNIMVTFKNQASR-PYSFYSSLISYKEDQRGEEPRRN-FVKPNETKIYFWKVQHHMAPTEDEFDCKAWAYFSDVDL 1830
Cdd:cd04229    78 AEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGAGdVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHVDV 157

                         170
                  ....*....|....
gi 569009643 1831 ERDMHSGLIGPLLI 1844
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.
 2176-2308 6.75e-30

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


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 116.01  E-value: 6.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  2176 QITASSYFTNmfaTWsPSQARLHLQGRTnAWRPQVNDPKQWLQVDLQKTMKVTGIITQGVKSlFTSMFVKEFLISSSQDG 2255
Cdd:pfam00754    1 QITASSSYSG---EG-PAAAALDGDPNT-AWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 569009643  2256 HHWTQILYNGkvFQGNQDSSTPMMNSLDPPLLTRYLRIHPQIW--EHQIALRLEI 2308
Cdd:pfam00754   75 ENWTTVKDEK--IPGNNDNNTPVTNTFDPPIKARYVRIVPTSWngGNGIALRAEL 127
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 213-346 2.69e-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: 2.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  213 YQFVLLFAVFDEGKSWHSETN------DSYTQSMDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEI 286
Cdd:cd11021     2 REFVLMFSVVDENLSWYLDENiktycsEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  287 HSIFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 346
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.
 2023-2153 2.64e-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: 105.99  E-value: 2.64e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  2023 QITASGHY-GQWAPNlARLHysGSIN-AWSTKE--PFSWIKVDLLAPMIVHGIKTQGaRQKFSSLYISQFIIMYSLDGKK 2098
Cdd:pfam00754    1 QITASSSYsGEGPAA-AALD--GDPNtAWSAWSgdDPQWIQVDLGKPKKITGVVTQG-RQDGSNGYVTSYKIEYSLDGEN 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009643  2099 WLSYQGNSTgtlmvfFGNVDSSGIKHNSFNPPIIARYIRLHPT--HSSIRSTLRMEL 2153
Cdd:pfam00754   77 WTTVKDEKI------PGNNDNNTPVTNTFDPPIKARYVRIVPTswNGGNGIALRAEL 127
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 214-349 3.50e-26

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 106.03  E-value: 3.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  214 QFVLLFAVFDEGKSWHSETN-DSYTQSMDSASARDWP-----KMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 287
Cdd:cd11022     3 EFFLLFTVFDENESWYLDENiQQFTLDPRSVDKEDEDfqesnKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009643  288 SIFLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKVDSC 349
Cdd:cd11022    83 GIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 589-727 1.12e-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: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  589 KRNVILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDF 667
Cdd:cd11012     2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQgLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009643  668 LSIFFSGYTF--KHKMVYE-DTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 727
Cdd:cd11012    82 HTAHFHGHSFdyKHRGVYRsDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 593-727 1.41e-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: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  593 ILFSIFDENQSWYITENMQRFLPNAAKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDFLSIF 671
Cdd:cd11018     6 LLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPgLVMAQHQRIRWHLLNMGSDEEIHSVH 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009643  672 FSGYTF------KHKM-VYedtlTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 727
Cdd:cd11018    86 FHGLPFtvrakkEYRMgVY----NLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1861-2003 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 569009643 1861 QEFALLFTIFDETKSWYFTENVKRNcktpcnfQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1940
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYSEVGERKS-------RDKFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009643 1941 QSIHFSGHVFTVRKkeeYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 2003
Cdd:cd11015    75 HSIFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1865-2005 4.02e-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: 97.25  E-value: 4.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1865 LLFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPgLVMAQDQRIRWYLLSMGNNENIQSIH 1944
Cdd:cd11016     6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009643 1945 FSGHVFtvrKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVYS 2005
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 ...
 1866-1983 1.20e-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: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1866 LFTIFDETKSWYFTENVKRNCKTPCNFQMEDPTLKENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENIQSIHF 1945
Cdd:cd14454     7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 569009643 1946 SGHVFTVRKKEEykmAVYNLYPGVFETLEMIPSRAGIW 1983
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 ...
 214-346 1.44e-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: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  214 QFVLLFAVFDEGKSWHSeTNDSyTQSMdsasardwpkMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFLEG 293
Cdd:cd14453     3 EYVLMFGVFDENKSWYK-QNAS-VDSV----------KYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNG 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 569009643  294 HTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 346
Cdd:cd14453    71 QVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 214-342 3.56e-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: 3.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  214 QFVLLFAVFDEGKSWHSETN-DSYTQ-----SMDSASARDWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 287
Cdd:cd11018     3 EFALLFTIFDETKSWYFEENmRRNCRppchiQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 569009643  288 SIFLEGHTFFVR---NHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEA 342
Cdd:cd11018    83 SVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSA 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1861-2003 4.88e-20

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 87.67  E-value: 4.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1861 QEFALLFTIFDEtkswyftENVKrncktpcnfqmedptlkENYRFHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1940
Cdd:cd11023     2 QEFIENSSIFLD-------LNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDF 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569009643 1941 QSIHFSGHvfTVRKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLV 2003
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 ...
 1861-1997 4.83e-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: 4.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1861 QEFALLFTIFDETKSWYFTENVKRNCKtpcnfqmedptlkenyrfHAINGYVMDTLPGLVMAQDQRIRWYLLSMGNNENI 1940
Cdd:cd14453     2 KEYVLMFGVFDENKSWYKQNASVDSVK------------------YTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPEL 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009643 1941 QSIHFSGHVFtvrKKEEYKMAVYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGM 1997
Cdd:cd14453    64 FSVHFNGQVL---EQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 214-346 7.64e-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: 7.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  214 QFVLLFAVFDEGKSWHSETN-DSYTQSMDSASARDWP-----KMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIH 287
Cdd:cd11012     3 EFALLFLVFDENESWYLDENiKTYSDHPEKVNKEDEEfiesnKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009643  288 SIFLEGHTF-FVRN--HRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKV 346
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 ...
 218-340 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 569009643  218 LFAVFDEGKSWHSETNDSYTQSMDSASARDWPK------MHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFL 291
Cdd:cd14454     7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKfyksniMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 569009643  292 EGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGM 340
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 ...
 592-727 2.33e-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: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  592 VILFSIFDENQSWYITENMQRflpNAAKTQPQDPGFQASNIMHSINGYVFDSLELTVCLHEVAYWHILSVGAQTDFLSIF 671
Cdd:cd14455     5 VLLFMTFDEEKSWYYEKNRKR---TCRENRVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVVH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 569009643  672 FSGYTFKHKMVYEDTLTLFPF---SGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 727
Cdd:cd14455    82 FHGQTFTEKGLKDHQLGVYPLlpgSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 592-727 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 569009643  592 VILFSIFDENQSWYiTENMQRflpnaaKTQPQDPGFQASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDFLSI 670
Cdd:cd11015     5 VLLFAVFDEGKSWY-SEVGER------KSRDKFKRADSRKEFHTINGYINASLPgLKICQRKPVIWHVIGMGTAPEVHSI 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569009643  671 FFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 727
Cdd:cd11015    78 FFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 216-349 1.41e-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: 75.67  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  216 VLLFAVFDEGKSWHSETNDSYTQSMDSASARDWPK------MHTVNGYVNRSLPGLIgCHRKSVYWHVIGMGTTPEIHSI 289
Cdd:cd11016     5 SLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDfyasnvMHTINGIVFDRRQFVI-CLTDVAYWYVLSVGAQTDFLSV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  290 FLEGHTFFVRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEAYVKVDSC 349
Cdd:cd11016    84 FFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 214-342 2.94e-15

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


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 74.90  E-value: 2.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  214 QFVLLFAVFDEGKSWHSETNDSYT---QSMDSASARDWPKMHTVNGYVnRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIF 290
Cdd:cd14455     3 EFVLLFMTFDEEKSWYYEKNRKRTcreNRVKDPNVQDNHTFHAINGII-YNLKGLRMYTNELVRWHLINMGGPKDLHVVH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569009643  291 LEGHTFF---VRNHRQASLEISPITFLTAQTLLIDLGQFLLFCHISSHKHDGMEA 342
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 ...
 588-727 3.86e-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: 3.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  588 DKRNVILFSIFDENQSWYitenmqrflpnaaKTQPQDPgfqasNIMHSINGYVFDSL-ELTVCLHEVAYWHILSVGAQTD 666
Cdd:cd14453     1 YKEYVLMFGVFDENKSWY-------------KQNASVD-----SVKYTINGYTNGTLpDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569009643  667 FLSIFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWVLGCHNSDFRKRGMTALLKV 727
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 628-727 1.55e-13

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 69.18  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  628 QASNIMHSINGYVFDSLE-LTVCLHEVAYWHILSVGAQTDFLSIFFSGYTFK-HKMVYEDTLTLFPFSGETVFMSMENPG 705
Cdd:cd11023    17 EEAGLMHSINGYVFGNLPgVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEaDKSRRTDVAELMPASMRVADMTAADVG 96

                          90       100
                  ....*....|....*....|..
gi 569009643  706 LWVLGCHNSDFRKRGMTALLKV 727
Cdd:cd11023    97 TWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 251-340 1.42e-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: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  251 MHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEIHSIFLEGHTFFVRNHRQASL-EISPITFLTAQTLLIDLGQFLLF 329
Cdd:cd11023    22 MHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRTDVaELMPASMRVADMTAADVGTWLLH 101

                          90
                  ....*....|.
gi 569009643  330 CHISSHKHDGM 340
Cdd:cd11023   102 CHVHDHYMAGM 112
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 219-350 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 569009643   219 FAVFDEGKSWHSETNDSYTQSMDsASARDWPKM------HTVNGYVNRSLPGLIGCHRKSVYWHVIgMGTTPEIHSIFLE 292
Cdd:pfam00394    1 EDYVITLSDWYHKDAKDLEKELL-ASGKAPTDFppvpdaVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569009643   293 GHTF--------FVRNHRQASLEISPITFLTAQ-TLLIDLGQFLLFCH-ISSHKHDGMEAYVKVDSCP 350
Cdd:pfam00394   79 GHKMtvvevdgvYVNPFTVDSLDIFPGQRYSVLvTANQDPGNYWIVASpNIPAFDNGTAAAILRYSGA 146
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 90-199 4.65e-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: 4.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   90 GLLGPTIWTEVHDTVVITLKN-MASHPVSLHAVGVSYWKASEGDEYEDQTSQMekeddkVFPGESHTYVWQVlkengpma 168
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQCP------IPPGESFTYRFTV-------- 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 569009643  169 sDPPCLTYSYMSHVDLvkDLNSGLIGALLVC 199
Cdd:cd04206    93 -DDQAGTFWYHSHVGG--QRADGLYGPLIVE 120
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1884-2007 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 569009643  1884 RNCKTPCNFQMEDPTLkeNYRFHAINGYVMD-TLPGLVMAQDQRIRWYLLsmgNNENI-QSIHFSGHVFTV-----RKKE 1956
Cdd:pfam07731    2 TPPKLPTLLQITSGNF--RRNDWAINGLLFPpNTNVITLPYGTVVEWVLQ---NTTTGvHPFHLHGHSFQVlgrggGPWP 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569009643  1957 EYKMAVYNL-----------YPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLFLVYSKQ 2007
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 ...
 93-198 4.09e-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: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   93 GPTIWTEVHDTVVITLKNMASHPVSLHAVGVSywkasegDEYEDQTSQMEkeddkVFPGESHTYVWQvlkengpmaSDPP 172
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIH-------DAAMDGTGLGP-----IMPGESFTYEFV---------AEPA 90

                          90       100
                  ....*....|....*....|....*..
gi 569009643  173 ClTYSYMSHVDLVKD-LNSGLIGALLV 198
Cdd:cd11024    91 G-THLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 469-572 8.08e-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: 8.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  469 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVSPLHArrlpRGIKHVKDLPIHPGEIFKYKWtvtvedgptKSDPRCl 548
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKM----DGVPGVTQPAIEPGESFTYKF---------KAERPG- 96

                          90       100
                  ....*....|....*....|....*
gi 569009643  549 TRYYSSFIN-PERDLASGLIGPLLI 572
Cdd:cd13859    97 TLWYHCHVNvNEHVGMRGMWGPLIV 121
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 466-573 1.53e-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: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  466 GLLGPLLYGEVGDTLLIIFKNQ-ASRPYNIYPHGItdvsplharRLPR-----GIKHVKDLPIHPGEIFKYKWTVtvedg 539
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGL---------RQPGtndgdGVAGLTQCPIPPGESFTYRFTV----- 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569009643  540 ptksDPRCLTRYYSSFINPERdlASGLIGPLLIC 573
Cdd:cd04206    93 ----DDQAGTFWYHSHVGGQR--ADGLYGPLIVE 120
rpoC2 CHL00117
RNA polymerase beta'' subunit; Reviewed
 1134-1509 2.53e-05

RNA polymerase beta'' subunit; Reviewed


Pssm-ID: 214368 [Multi-domain]  Cd Length: 1364  Bit Score: 49.94  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1134 NGNNSLNSEQEHSPKQLVYLMFKKYVKNQSFLSEKNKVTVEqdgFTKNIGLKdmafphnmSIFLTTLSNVHENGRHNQEK 1213
Cdd:CHL00117  741 PGTGKKNSKESKKIKNWIYVQRITPTKKKYFVLVRPVVTYE---IADGINLA--------TLFPQDLLQEKDNLQLRVVN 809

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1214 NIQEEIEKEalIEEkvvlpqvheaTGSKNFLKDILILGTRQ---NISLYEVH---VPVLQNitsiNNSTNTVQIHM--EH 1285
Cdd:CHL00117  810 YILYGNGKP--IRG----------ISSIQLVRTCLVLNWDQdkkSSSIEEARasfVEVRTN----GLIRDFLRINLvkSP 873

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1286 FFKRRKDKETNSEGLVNKTremvKNYPSQKNIttqrskraLGQFRLSTQWLKTincsTQCIIKQI-DHSKEMKKFITKSS 1364
Cdd:CHL00117  874 ISYIRKRNDPSSSGLLVQS----NNFLDSTNI--------YSKAEIQSQSLSQ----NQGTIRTLlNRNKESQSLLILSS 937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1365 lSDSSVIKSTTQTNSSDSHIVKTSAFPPIDLKRSPFQNKFSHVQASSYIYDFKTKSSRIqesNNFLKETKINNPSLAILP 1444
Cdd:CHL00117  938 -SDCFRIGPFNGKKSKYHNIKESNPLIPIRNSLGPLGTVLQIANFSSSYHLLTHNQILV---TKYLQLDNLKQTFQVKVL 1013

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569009643 1445 WNMFIDQ-GKFTSPgKSNTNSVTYKKRENIIFLKPTLPEESGKIELLPQvSIQEEEILPTETSHGS 1509
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 ...
 1892-2001 3.74e-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: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643 1892 FQMEDPTLKENYRFHAINGYVMDTLPG----LVMAQDQRIRWYLLSMGNNENIQSIHFSGHVFTV----------RKKEE 1957
Cdd:cd04207     6 LVLSQTGAPDGTTRWVINGMPFKEGDAntdiFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFWVlgsgggpfdaPLNLT 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 569009643 1958 YKMA--VYNLYPGVFETLEMIPSRAGIWRVECLIGEHLQAGMSTLF 2001
Cdd:cd04207    86 NPPWrdTVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 452-572 8.28e-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: 8.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  452 DETFKTRETIQHESGLLGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplharRLPR---GIKHVKDLPIHPGEIF 528
Cdd:cd13861    14 DLGGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL---------RLPNamdGVPGLTQPPVPPGESF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 569009643  529 KYKWTVtvedgPtksDPRclTRYYSSFINPERDLASGLIGPLLI 572
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 ...
 469-572 1.06e-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: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  469 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksdpr 546
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGL------FQNGTNwmDGTAGITQCPIPPGGSFTYNFTVDGQYG------- 96

                          90       100
                  ....*....|....*....|....*.
gi 569009643  547 clTRYYSSFINPErdLASGLIGPLLI 572
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 ...
 469-572 2.12e-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: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  469 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksdpr 546
Cdd:cd13850    28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGI------LQRGTPwsDGVPGVTQWPIQPGGSFTYRWKAEDQYG------- 94

                          90       100
                  ....*....|....*....|....*.
gi 569009643  547 clTRYYSSFINPErdLASGLIGPLLI 572
Cdd:cd13850    95 --LYWYHSHYRGY--YMDGLYGPIYI 116
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 90-198 3.67e-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: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   90 GLLGPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGDEYEDQtsqmekedDKVFPGESHTYVWQVlkengpmas 169
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGLTQ--------PPVPPGESFTYEFTP--------- 90

                          90       100
                  ....*....|....*....|....*....
gi 569009643  170 dPPCLTYSYMSHVDLVKDLNSGLIGALLV 198
Cdd:cd13861    91 -PDAGTYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 93-198 6.32e-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: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   93 GPTIWTEVHDTVVITLKNMASHPVSLHAVGVSywkaSEGDEYEDQT---SQMEkeddkVFPGESHTYVWQVLKENGpmas 169
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGTagiTQCP-----IPPGGSFTYNFTVDGQYG---- 96

                          90       100
                  ....*....|....*....|....*....
gi 569009643  170 dppclTYSYMSHVDLvkDLNSGLIGALLV 198
Cdd:cd13857    97 -----TYWYHSHYST--QYADGLVGPLIV 118
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 93-198 8.42e-04

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: 41.87  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   93 GPTIWTEVHDTVVITLKNMASHPVSLHAVGVSYWKASEGdeyedqtSQMEKEDdkVFPGESHTYVWQVLK----ENGPMA 168
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDG-------TGMNASI--VAPGDTRIYTWRTHGgyrrADGSWA 99

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569009643  169 SDPPClTYSYMSHV----DLVKDLNSGLIGALLV 198
Cdd:cd14449   100 EGTAG-YWHYHDHVfgteHGTEGLSRGLYGALIV 132
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 440-539 9.01e-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: 9.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   440 RKYK-KVRFIAYTdETFKTRETIQHESGLLGPLLYGEVGDTLLIIFKNQASrpYNIYPHgitdvspLHARRLPR-----G 513
Cdd:TIGR03389    4 RHYTfDVQEKNVT-RLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQ--YNVTIH-------WHGVRQLRngwadG 73

                           90       100
                   ....*....|....*....|....*.
gi 569009643   514 IKHVKDLPIHPGEIFKYKWTVTVEDG 539
Cdd:TIGR03389   74 PAYITQCPIQPGQSYVYNFTITGQRG 99
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 467-572 2.37e-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: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   467 LLGPLLYGEVGDTLLIIFKNQASRPYNIYPHGItdvsplHARRLP--RGIKHVKDLPIHPGEIFKYKWTVTVEDGptksd 544
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGL------QQRGTPwmDGVPGVTQCPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*...
gi 569009643   545 prclTRYYSSFINPERdlASGLIGPLLI 572
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 ...
 469-535 2.54e-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: 2.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569009643  469 GPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVSplharrlprgIKHVKDLPIHPGEIFKYKWTVT 535
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAA----------MDGTGLGPIMPGESFTYEFVAE 88
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 93-198 2.90e-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: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643   93 GPTIWTEVHDTVVITLKN-MASHPVSLHAVGV----SYWkaSEGDEYEDQTSQMekeddkvfPGESHTYVWQVlkengpm 167
Cdd:cd13845    30 GPTIRATAGDTIVVELENkLPTEGVAIHWHGIrqrgTPW--ADGTASVSQCPIN--------PGETFTYQFVV------- 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 569009643  168 asDPPClTYSYMSHVDLVKdlNSGLIGALLV 198
Cdd:cd13845    93 --DRPG-TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 633-728 9.32e-03

The second 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. The biological function of McoN 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: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 38.77  E-value: 9.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569009643  633 MHSINGYVFDSLE-LTVCLHEVAYWHIlsVGAQTDFLSIFFSGYTFK-----------HKMVYEDTLTLFPfsGET--VF 698
Cdd:cd04202    29 YFTINGKSFPATPpLVVKEGDRVRIRL--INLSMDHHPMHLHGHFFLvtatdggpipgSAPWPKDTLNVAP--GERydIE 104

                          90       100       110
                  ....*....|....*....|....*....|....
gi 569009643  699 MSMENPGLWVLGCHNSDF----RKRGMTALLKVS 728
Cdd:cd04202   105 FVADNPGDWMFHCHKLHHamngMGGGMMTLIGYE 138
 
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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