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Conserved domains on  [gi|88758619|gb|AAI13358|]
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Coagulation factor V (proaccelerin, labile factor), partial [synthetic construct]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 348-528 1.81e-118

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: 371.90  E-value: 1.81e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  348 KRWEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIGKHYKKVMYTQYEDESFTKHTVNPNMKEDGILGPIIRAQV 427
Cdd:cd14450    1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILGPVIRAQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  428 RDTLKIVFKNMASRPYSIYPHGVTFSPYEDEVNSSFTSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYS 507
Cdd:cd14450   81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHS 160

                        170       180
                 ....*....|....*....|.
gi 88758619  508 DVDIMRDIASGLIGLLLICKS 528
Cdd:cd14450  161 AVDITRDIASGLIGPLLICKS 181
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1579-1754 2.46e-112

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: 353.76  E-value: 2.46e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1579 RRNYYIAAEEISWDYSEFVQRETDiedSDDIPEDTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILGPIIRAEVDDVIQV 1658
Cdd:cd14451    1 KRRYYIAAEEEEWDYAGYGKSRLD---KTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1659 RFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSAVNPEK 1738
Cdd:cd14451   78 FFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEK 157

                        170
                 ....*....|....*.
gi 88758619 1739 DIHSGLIGPLLICQKG 1754
Cdd:cd14451  158 DIHSGLIGPLLICRKG 173
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 32-196 1.71e-96

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


The actual alignment was detected with superfamily member cd04226:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 165  Bit Score: 308.33  E-value: 1.71e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   32 RQFYVAAQGISWSYRPEPTNSSLNLSVTSFKKIVYREYEPYFKKEKPQSTISGLLGPTLYAEVGDIIKVHFKNKADKPLS 111
Cdd:cd04226    1 REYYIAAQNIDWDYTPQSEELRLKRSEQSFKKIVYREYEEGFKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  112 IHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFNSGLIGPLL 191
Cdd:cd04226   81 IHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALL 160


                 ....*
gi 88758619  192 ICKKG 196
Cdd:cd04226  161 ICKKG 165
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 541-684 1.45e-90

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: 290.23  E-value: 1.45e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  541 DIEQQAVFAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNE 620
Cdd:cd14454    1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88758619  621 ILTIHFTGHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRDVKC 684
Cdd:cd14454   81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1766-1902 3.49e-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 cd14455:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 140  Bit Score: 260.57  E-value: 3.49e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1766 MREFVLLFMTFDEKKSWYYEKKSRSSWR---LTSSEMKKSHEFHAINGMIYSLPGLKMYEQEWVRLHLLNIGGSQDIHVV 1842
Cdd:cd14455    1 RREFVLLFMTFDEEKSWYYEKNRKRTCRenrVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1843 HFHGQTLLENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLI 1902
Cdd:cd14455   81 HFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 208-326 8.81e-66

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


The actual alignment was detected with superfamily member cd14453:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 123  Bit Score: 218.57  E-value: 8.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  208 DKQIVLLFAVFDES----KSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKV 283
Cdd:cd14453    1 YKEYVLMFGVFDENkswyKQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNGQVLEQNGHKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 88758619  284 SAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDI 326
Cdd:cd14453   81 SAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2068-2220 5.77e-56

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


:

Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 191.41  E-value: 5.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 2068 TPLGMENGKiENKQITASSfkksWWGDYWEPFRARLNaqgRVNAWQAKANNNKQWLEIDLLKIKKITAIITQGCKSLSSE 2147
Cdd:cd00057    1 EPLGMESGL-ADDQITASS----SYSSGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88758619 2148 MYVKSYTIHYSEQGVEWKPYRLKssMVDKIFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWNQSIALRLELFG 2220
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1909-2060 5.96e-46

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: 162.52  E-value: 5.96e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1909 MPMGLSTGIiSDSQIKASEFLGY-WEPRLARLNnggSYNAWSveklAAEFASKPWIQVDMQKEVIITGIQTQGAKHYLKS 1987
Cdd:cd00057    1 EPLGMESGL-ADDQITASSSYSSgWEASRARLN---SDNAWT----PAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88758619 1988 CYTTEFYVAYSSNQINWQIFKGNStrNVMYFNGNSDASTIKENQFDPPIVARYIRISPTRAYNRPTLRLELQG 2060
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDKG--EEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
YjbI COG1357
Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];
1234-1421 1.69e-04

Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];


:

Pssm-ID: 440968 [Multi-domain]  Cd Length: 178  Bit Score: 44.55  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1234 DLSHTTLS-PDLSHTTLS-LDLSQTNLSPELSQTNLSPAlgqmplspDLSHTTLS-LDFSQTNLSP-ELSHMTLS-PELS 1308
Cdd:COG1357    1 DLSGADLSgADLSGADLSgADLSGANLSGALSGANLSGA--------NLSGANLTgANLSGADLSGaDLSGANLSgADLS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1309 QTNLSPAlgqmpispDLSHTTLsLDFSQTNLSP-ELSQTNLSPAlgqmplspDPSHTTLS-LDLSQTNLS-PELSQTNLS 1385
Cdd:COG1357   73 GANLTGA--------DLSGANL-ANLSGANLSGaNLSGANLRGA--------NLSGANLSgADLSGADLSgANLSGADLS 135

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 88758619 1386 P-DLSEmplfADLSQIpltpDLDQMTLSP-DLGETDLS 1421
Cdd:COG1357  136 GaNLSG----ANLSGA----DLSGADLSGaNLSGANLS 165
 
Name Accession Description Interval E-value
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 348-528 1.81e-118

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: 371.90  E-value: 1.81e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  348 KRWEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIGKHYKKVMYTQYEDESFTKHTVNPNMKEDGILGPIIRAQV 427
Cdd:cd14450    1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILGPVIRAQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  428 RDTLKIVFKNMASRPYSIYPHGVTFSPYEDEVNSSFTSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYS 507
Cdd:cd14450   81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHS 160

                        170       180
                 ....*....|....*....|.
gi 88758619  508 DVDIMRDIASGLIGLLLICKS 528
Cdd:cd14450  161 AVDITRDIASGLIGPLLICKS 181
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1579-1754 2.46e-112

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: 353.76  E-value: 2.46e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1579 RRNYYIAAEEISWDYSEFVQRETDiedSDDIPEDTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILGPIIRAEVDDVIQV 1658
Cdd:cd14451    1 KRRYYIAAEEEEWDYAGYGKSRLD---KTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1659 RFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSAVNPEK 1738
Cdd:cd14451   78 FFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEK 157

                        170
                 ....*....|....*.
gi 88758619 1739 DIHSGLIGPLLICQKG 1754
Cdd:cd14451  158 DIHSGLIGPLLICRKG 173
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 32-196 1.71e-96

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: 308.33  E-value: 1.71e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   32 RQFYVAAQGISWSYRPEPTNSSLNLSVTSFKKIVYREYEPYFKKEKPQSTISGLLGPTLYAEVGDIIKVHFKNKADKPLS 111
Cdd:cd04226    1 REYYIAAQNIDWDYTPQSEELRLKRSEQSFKKIVYREYEEGFKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  112 IHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFNSGLIGPLL 191
Cdd:cd04226   81 IHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALL 160


                 ....*
gi 88758619  192 ICKKG 196
Cdd:cd04226  161 ICKKG 165
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 541-684 1.45e-90

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: 290.23  E-value: 1.45e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  541 DIEQQAVFAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNE 620
Cdd:cd14454    1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88758619  621 ILTIHFTGHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRDVKC 684
Cdd:cd14454   81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1766-1902 3.49e-80

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: 260.57  E-value: 3.49e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1766 MREFVLLFMTFDEKKSWYYEKKSRSSWR---LTSSEMKKSHEFHAINGMIYSLPGLKMYEQEWVRLHLLNIGGSQDIHVV 1842
Cdd:cd14455    1 RREFVLLFMTFDEEKSWYYEKNRKRTCRenrVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1843 HFHGQTLLENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLI 1902
Cdd:cd14455   81 HFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 208-326 8.81e-66

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: 218.57  E-value: 8.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  208 DKQIVLLFAVFDES----KSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKV 283
Cdd:cd14453    1 YKEYVLMFGVFDENkswyKQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNGQVLEQNGHKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 88758619  284 SAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDI 326
Cdd:cd14453   81 SAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2068-2220 5.77e-56

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


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 191.41  E-value: 5.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 2068 TPLGMENGKiENKQITASSfkksWWGDYWEPFRARLNaqgRVNAWQAKANNNKQWLEIDLLKIKKITAIITQGCKSLSSE 2147
Cdd:cd00057    1 EPLGMESGL-ADDQITASS----SYSSGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88758619 2148 MYVKSYTIHYSEQGVEWKPYRLKssMVDKIFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWNQSIALRLELFG 2220
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1909-2060 5.96e-46

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: 162.52  E-value: 5.96e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1909 MPMGLSTGIiSDSQIKASEFLGY-WEPRLARLNnggSYNAWSveklAAEFASKPWIQVDMQKEVIITGIQTQGAKHYLKS 1987
Cdd:cd00057    1 EPLGMESGL-ADDQITASSSYSSgWEASRARLN---SDNAWT----PAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88758619 1988 CYTTEFYVAYSSNQINWQIFKGNStrNVMYFNGNSDASTIKENQFDPPIVARYIRISPTRAYNRPTLRLELQG 2060
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDKG--EEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1906-2061 3.74e-37

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: 137.26  E-value: 3.74e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619    1906 DCRMPMGLStgiiSDSQIKASEflGYWEPRLARLNnGGSYNAWSveklAAEFASKPWIQVDMQKEVIITGIQTQGAKHYL 1985
Cdd:smart00231    1 PCNEPLGLE----SDSQITASS--SYWAAKIARLN-GGSDGGWC----PAKNDLPPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88758619    1986 KScytTEFYVAYSSNQINWQIFKGnstRNVMYFNGNSDASTIKENQFDPPIVARYIRISPTRAYNRPTLRLELQGC 2061
Cdd:smart00231   70 DW---VTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2065-2221 6.78e-34

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


Pssm-ID: 214572  Cd Length: 139  Bit Score: 128.01  E-value: 6.78e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619    2065 GCSTPLGMENgkieNKQITASSfkkswwgDYWEPFRARLNaQGRVNAWQAKANNNKQWLEIDLLKIKKITAIITQGCKSL 2144
Cdd:smart00231    1 PCNEPLGLES----DSQITASS-------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHGN 68

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88758619    2145 SSEMYvksYTIHYSEQGVEWKPYRLKSSMVdkiFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWNQSIALRLELFGC 2221
Cdd:smart00231   69 GDWVT---YKLEYSDDGVNWTTYKDGNSKV---FPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2081-2218 1.34e-31

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: 121.02  E-value: 1.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   2081 QITASSFkkswWGDYWEPfRARLNaqGRVN-AWQAKANNNKQWLEIDLLKIKKITAIITQGCKSLSSeMYVKSYTIHYSE 2159
Cdd:pfam00754    1 QITASSS----YSGEGPA-AAALD--GDPNtAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSN-GYVTSYKIEYSL 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88758619   2160 QGVEWKPYRlkssmvDKIFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWN--QSIALRLEL 2218
Cdd:pfam00754   73 DGENWTTVK------DEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNggNGIALRAEL 127
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1922-2058 1.11e-24

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: 101.37  E-value: 1.11e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   1922 QIKASEFLGYWEPRLARLNNGGSyNAWSveklAAEFASKPWIQVDMQKEVIITGIQTQGAKHyLKSCYTTEFYVAYSSNQ 2001
Cdd:pfam00754    1 QITASSSYSGEGPAAAALDGDPN-TAWS----AWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 88758619   2002 INWQIFKGNSTrnvmyfNGNSDASTIKENQFDPPIVARYIRISPTRA--YNRPTLRLEL 2058
Cdd:pfam00754   75 ENWTTVKDEKI------PGNNDNNTPVTNTFDPPIKARYVRIVPTSWngGNGIALRAEL 127
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 85-192 1.05e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 59.95  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   85 LLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYsklsegasyldhtfPAEkMD----DAVAPGREYTYEWSIsedsgp 160
Cdd:COG2132   42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRV--------------PNA-MDgvpgDPIAPGETFTYEFPV------ 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 88758619  161 thDDPPClTHIYYSHENLIEDFN--SGLIGPLLI 192
Cdd:COG2132  101 --PQPAG-TYWYHPHTHGSTAEQvyRGLAGALIV 131
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 81-192 1.58e-08

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: 54.56  E-value: 1.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619     81 TISG-LLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSK--LSEGASYLDHtfpaekmdDAVAPGREYTYEWSISED 157
Cdd:pfam07732   19 GVNGqFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGtpWMDGVPGVTQ--------CPIPPGQSFTYRFQVKQQ 90

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 88758619    158 SGpthddppclTHIYYSHENLIEdfNSGLIGPLLI 192
Cdd:pfam07732   91 AG---------TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1643-1867 6.89e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 57.25  E-value: 6.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1643 ILGPIIRAEVDDVIQVRFKNLASRPYSLHAHGL--SYEkssegktyEDDSPEwfkedNAVQPNSSYTYVWHATERSG--- 1717
Cdd:COG2132   42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLrvPNA--------MDGVPG-----DPIAPGETFTYEFPVPQPAGtyw 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1718 --PESPGSacrawayySAVNpekdIHSGLIGPLLIcqkgilH-KDSNMPMDMREFVLLF--MTFDEKKSWYYekksrssw 1792
Cdd:COG2132  109 yhPHTHGS--------TAEQ----VYRGLAGALIV------EdPEEDLPRYDRDIPLVLqdWRLDDDGQLLY-------- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1793 RLTSSEMKKSHEFHAINGMIysLPGLKMYEQEWVRLHLLNIGGS----------QDIHVVHFHGQTLlengNKQHQLGVW 1862
Cdd:COG2132  163 PMDAAMGGRLGDTLLVNGRP--NPTLEVRPGERVRLRLLNASNAriyrlalsdgRPFTVIATDGGLL----PAPVEVDEL 236


                 ....*
gi 88758619 1863 PLLPG 1867
Cdd:COG2132  237 LLAPG 241
YjbI COG1357
Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];
1234-1421 1.69e-04

Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];


Pssm-ID: 440968 [Multi-domain]  Cd Length: 178  Bit Score: 44.55  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1234 DLSHTTLS-PDLSHTTLS-LDLSQTNLSPELSQTNLSPAlgqmplspDLSHTTLS-LDFSQTNLSP-ELSHMTLS-PELS 1308
Cdd:COG1357    1 DLSGADLSgADLSGADLSgADLSGANLSGALSGANLSGA--------NLSGANLTgANLSGADLSGaDLSGANLSgADLS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1309 QTNLSPAlgqmpispDLSHTTLsLDFSQTNLSP-ELSQTNLSPAlgqmplspDPSHTTLS-LDLSQTNLS-PELSQTNLS 1385
Cdd:COG1357   73 GANLTGA--------DLSGANL-ANLSGANLSGaNLSGANLRGA--------NLSGANLSgADLSGADLSgANLSGADLS 135

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 88758619 1386 P-DLSEmplfADLSQIpltpDLDQMTLSP-DLGETDLS 1421
Cdd:COG1357  136 GaNLSG----ANLSGA----DLSGADLSGaNLSGANLS 165
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 408-487 1.92e-04

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 43.00  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619    408 TVNpnmkeDGILGPIIRAQVRDTLKIVFKNMASRPYSIYPHG--VTFSPYEDEVNssftsGRNNTMIravQPGETYTYKW 485
Cdd:pfam07732   19 GVN-----GQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGlqQRGTPWMDGVP-----GVTQCPI---PPGQSFTYRF 85


                   ..
gi 88758619    486 NI 487
Cdd:pfam07732   86 QV 87
PLN02191 PLN02191
L-ascorbate oxidase
 75-192 3.87e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 45.39  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619    75 KEKPQSTISGLL-GPTLYAEVGDIIKVHFKNK-ADKPLSIHPQGIRY--SKLSEGASYLDHTfpaekmddAVAPGREYTY 150
Cdd:PLN02191   40 KEGAVMTVNGQFpGPTIDAVAGDTIVVHLTNKlTTEGLVIHWHGIRQkgSPWADGAAGVTQC--------AINPGETFTY 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 88758619   151 EWSIsEDSGpthddppclTHIYYSHENLIEdfNSGLIGPLLI 192
Cdd:PLN02191  112 KFTV-EKPG---------THFYHGHYGMQR--SAGLYGSLIV 141
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 75-192 9.89e-04

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 44.36  E-value: 9.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619     75 KEKPQSTISGLL-GPTLYAEVGDIIKVHFKNK-ADKPLSIHPQGIRysklSEGASYLDHTfpAEKMDDAVAPGREYTYEW 152
Cdd:TIGR03388   18 FEKLVIGINGQFpGPTIRAQAGDTIVVELTNKlHTEGVVIHWHGIR----QIGTPWADGT--AGVTQCAINPGETFIYNF 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 88758619    153 SIsedsgpthDDPPclTHIYYSHENLIEdfNSGLIGPLLI 192
Cdd:TIGR03388   92 VV--------DRPG--TYFYHGHYGMQR--SAGLYGSLIV 119
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1794-1906 1.03e-03

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 41.27  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   1794 LTSSEMKKSheFHAINGMIYSL--PGLKMYEQEWVRLHLLNigGSQDIHVVHFHGQT--LLENGNKQHQL---------- 1859
Cdd:pfam07731   12 ITSGNFRRN--DWAINGLLFPPntNVITLPYGTVVEWVLQN--TTTGVHPFHLHGHSfqVLGRGGGPWPEedpktynlvd 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 88758619   1860 GVW----PLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLIMDRD 1906
Cdd:pfam07731   88 PVRrdtvQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1643-1717 3.38e-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: 39.54  E-value: 3.38e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88758619   1643 ILGPIIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSegktYEDDSPEWfkEDNAVQPNSSYTYVWHATERSG 1717
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTP----WMDGVPGV--TQCPIPPGQSFTYRFQVKQQAG 92
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 548-670 5.31e-03

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: 39.61  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619    548 FAVFDENKSWYlEDNINKFCENPDEVKRDDPKFyeSNIMS--TINGYVPESITTLGFCFDDTVQWHFCSVGTQNEiLTIH 625
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDF--PPVPDavLINGKDGASLATLTVTPGKTYRLRIINVALDDS-LNFS 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 88758619    626 FTGHSFIY----GKRHE----DTLTLFPmrGE--SVTVTMDN-VGT-WMLTSMNSSP 670
Cdd:pfam00394   77 IEGHKMTVvevdGVYVNpftvDSLDIFP--GQrySVLVTANQdPGNyWIVASPNIPA 131
 
Name Accession Description Interval E-value
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 348-528 1.81e-118

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: 371.90  E-value: 1.81e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  348 KRWEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIGKHYKKVMYTQYEDESFTKHTVNPNMKEDGILGPIIRAQV 427
Cdd:cd14450    1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILGPVIRAQV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  428 RDTLKIVFKNMASRPYSIYPHGVTFSPYEDEVNSSFTSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYS 507
Cdd:cd14450   81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHS 160

                        170       180
                 ....*....|....*....|.
gi 88758619  508 DVDIMRDIASGLIGLLLICKS 528
Cdd:cd14450  161 AVDITRDIASGLIGPLLICKS 181
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1579-1754 2.46e-112

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: 353.76  E-value: 2.46e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1579 RRNYYIAAEEISWDYSEFVQRETDiedSDDIPEDTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILGPIIRAEVDDVIQV 1658
Cdd:cd14451    1 KRRYYIAAEEEEWDYAGYGKSRLD---KTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1659 RFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSAVNPEK 1738
Cdd:cd14451   78 FFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEK 157

                        170
                 ....*....|....*.
gi 88758619 1739 DIHSGLIGPLLICQKG 1754
Cdd:cd14451  158 DIHSGLIGPLLICRKG 173
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 32-196 1.71e-96

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: 308.33  E-value: 1.71e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   32 RQFYVAAQGISWSYRPEPTNSSLNLSVTSFKKIVYREYEPYFKKEKPQSTISGLLGPTLYAEVGDIIKVHFKNKADKPLS 111
Cdd:cd04226    1 REYYIAAQNIDWDYTPQSEELRLKRSEQSFKKIVYREYEEGFKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  112 IHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFNSGLIGPLL 191
Cdd:cd04226   81 IHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALL 160


                 ....*
gi 88758619  192 ICKKG 196
Cdd:cd04226  161 ICKKG 165
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 350-528 1.89e-94

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: 302.79  E-value: 1.89e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  350 WEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIGKHYKKVMYTQYEDESFTKHtvNPNMKEDGILGPIIRAQVRD 429
Cdd:cd04199    1 RHYYIAAEEIDWDYAPSGLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTP--GPQPEHLGILGPTIRAEVGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  430 TLKIVFKNMASRPYSIYPHGVTFSPYEDEVNSSFTSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYSDV 509
Cdd:cd04199   79 TIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHV 158

                        170
                 ....*....|....*....
gi 88758619  510 DIMRDIASGLIGLLLICKS 528
Cdd:cd04199  159 DLEKDINSGLIGPLLICKK 177
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 541-684 1.45e-90

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: 290.23  E-value: 1.45e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  541 DIEQQAVFAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNE 620
Cdd:cd14454    1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88758619  621 ILTIHFTGHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRDVKC 684
Cdd:cd14454   81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 1580-1753 1.12e-86

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: 280.45  E-value: 1.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1580 RNYYIAAEEISWDYSEFVQRETDIE------DSDDIPEDTTYKKVVFRKYLDSTFTKRdprGEYEEHLGILGPIIRAEVD 1653
Cdd:cd04199    1 RHYYIAAEEIDWDYAPSGLAEKDLSyrnqylDNGPFRIGRSYKKVVYREYTDESFTTP---GPQPEHLGILGPTIRAEVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1654 DVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSA 1733
Cdd:cd04199   78 DTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSH 157

                        170       180
                 ....*....|....*....|
gi 88758619 1734 VNPEKDIHSGLIGPLLICQK 1753
Cdd:cd04199  158 VDLEKDINSGLIGPLLICKK 177
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1766-1902 3.49e-80

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: 260.57  E-value: 3.49e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1766 MREFVLLFMTFDEKKSWYYEKKSRSSWR---LTSSEMKKSHEFHAINGMIYSLPGLKMYEQEWVRLHLLNIGGSQDIHVV 1842
Cdd:cd14455    1 RREFVLLFMTFDEEKSWYYEKNRKRTCRenrVKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1843 HFHGQTLLENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLI 1902
Cdd:cd14455   81 HFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 32-195 3.43e-75

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: 247.70  E-value: 3.43e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   32 RQFYVAAQGISWSYRPEPT------------NSSLNLSVTSFKKIVYREYEPY-FKKEKPQSTISGLLGPTLYAEVGDII 98
Cdd:cd04199    1 RHYYIAAEEIDWDYAPSGLaekdlsyrnqylDNGPFRIGRSYKKVVYREYTDEsFTTPGPQPEHLGILGPTIRAEVGDTI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   99 KVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENL 178
Cdd:cd04199   81 KVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHVDL 160

                        170
                 ....*....|....*..
gi 88758619  179 IEDFNSGLIGPLLICKK 195
Cdd:cd04199  161 EKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 541-681 1.48e-66

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 221.51  E-value: 1.48e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  541 DIEQQAVFAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNE 620
Cdd:cd04200    1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88758619  621 ILTIHFTGHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRD 681
Cdd:cd04200   81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 208-326 8.81e-66

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: 218.57  E-value: 8.81e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  208 DKQIVLLFAVFDES----KSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKV 283
Cdd:cd14453    1 YKEYVLMFGVFDENkswyKQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNGQVLEQNGHKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 88758619  284 SAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDI 326
Cdd:cd14453   81 SAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1577-1759 2.29e-64

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: 217.73  E-value: 2.29e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1577 GNRRNYYIAAEEISWDYS-----EFVQRETDIEDSDDIP----EDT----TYKKVVFRKYLDSTFTKRDPRGEYEEHLGI 1643
Cdd:cd04224    1 GKVRHYFIAAEEIMWDYApsgknLFTGQNLTAPGSDSEVffqrNETriggTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1644 LGPIIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPewfKEDNAVQPNSSYTYVWHATERSGPESPGS 1723
Cdd:cd04224   81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDP---SPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 88758619 1724 ACRAWAYYSAVNPEKDIHSGLIGPLLICQKGILHKD 1759
Cdd:cd04224  158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNAN 193
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 348-527 5.05e-59

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: 201.31  E-value: 5.05e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  348 KRWEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIGKHYKKVMYTQYEDESFTKHtvNPNMKEDGILGPIIRAQV 427
Cdd:cd04227    1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRR--EAKQTEKGILGPLLKGEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  428 RDTLKIVFKNMASRPYSIYPHGVT-FSPYEDEVNSsftSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYY 506
Cdd:cd04227   79 GDQIHIMFKNTASRPYNIYPHGLTsVRPMYRSRNP---AGEKDLKTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQ 155

                        170       180
                 ....*....|....*....|.
gi 88758619  507 SDVDIMRDIASGLIGLLLICK 527
Cdd:cd04227  156 STVDPERDLASGLIGPLLICK 176
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 30-205 1.54e-56

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: 195.00  E-value: 1.54e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   30 QLRQFYVAAQGISWSYRPEPTNSSLNLSVT-------------------SFKKIVYREY-EPYFKKEKPQSTIS---GLL 86
Cdd:cd04224    2 KVRHYFIAAEEIMWDYAPSGKNLFTGQNLTapgsdsevffqrnetriggTYWKVRYVEYtDATFTTRKHRSKEEehlGIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   87 GPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHT-FPAEKmddaVAPGREYTYEWSISEDSGPTHDDP 165
Cdd:cd04224   82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDpSPGSH----VSPGETFTYEWTVPEGVGPTNQDP 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 88758619  166 PCLTHIYYSHENLIEDFNSGLIGPLLICKKGTLTEGGTQK 205
Cdd:cd04224  158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2068-2220 5.77e-56

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


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 191.41  E-value: 5.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 2068 TPLGMENGKiENKQITASSfkksWWGDYWEPFRARLNaqgRVNAWQAKANNNKQWLEIDLLKIKKITAIITQGCKSLSSE 2147
Cdd:cd00057    1 EPLGMESGL-ADDQITASS----SYSSGWEASRARLN---SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88758619 2148 MYVKSYTIHYSEQGVEWKPYRLKssMVDKIFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWNQSIALRLELFG 2220
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1580-1753 1.10e-54

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: 188.83  E-value: 1.10e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1580 RNYYIAAEEISWDYSEfvQRETDIE--------------DSDDIPEDTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILG 1645
Cdd:cd04225    1 RTYYIAAEEVEWDYSP--QRTWEQElhntheespgnaflNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1646 PIIRAEVDDVIQVRFKNLASRPYSLHAHGLsyekssegKTyedDSPewfkEDNAVQPNSSYTYVWHATERSGPESPGSAC 1725
Cdd:cd04225   79 PLIHAEVGEKVKIVFKNMASRPYSIHAHGV--------KT---DSS----WVAPTEPGETQTYTWKIPERSGPGVEDSNC 143

                        170       180
                 ....*....|....*....|....*...
gi 88758619 1726 RAWAYYSAVNPEKDIHSGLIGPLLICQK 1753
Cdd:cd04225  144 ISWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 352-538 1.58e-54

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 189.22  E-value: 1.58e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  352 YFIAAEEVIWDYAP-----------VIPANMDKKYRSQHldnfSNQIGKHYKKVMYTQYEDESFTKHTvnPNMKED---G 417
Cdd:cd04224    6 YFIAAEEIMWDYAPsgknlftgqnlTAPGSDSEVFFQRN----ETRIGGTYWKVRYVEYTDATFTTRK--HRSKEEehlG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  418 ILGPIIRAQVRDTLKIVFKNMASRPYSIYPHGVTFspyedEVNSSFTSGRNNTMIRA--VQPGETYTYKWNILEFDEPTE 495
Cdd:cd04224   80 ILGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFY-----EKNYEGAMYRDGDPSPGshVSPGETFTYEWTVPEGVGPTN 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 88758619  496 NDAQCLTRPYYSDVDIMRDIASGLIGLLLICKSRSLDRQGIQR 538
Cdd:cd04224  155 QDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1580-1754 1.68e-53

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 185.48  E-value: 1.68e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1580 RNYYIAAEEISWDY----SEFVQRETDIEDSDDIPEdTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILGPIIRAEVDDV 1655
Cdd:cd04228    2 RHYFIAAVEVLWDYgmqrPQHFLRARDPNRGRRKSV-PQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVEDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1656 IQVRFKNLASRPYSLHAHGLSYEkssegktyEDDSPEWFKedNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSAVN 1735
Cdd:cd04228   81 IMVTFKNLASRPYSFHSSLISYE--------EDQRAEPRG--NFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVD 150

                        170
                 ....*....|....*....
gi 88758619 1736 PEKDIHSGLIGPLLICQKG 1754
Cdd:cd04228  151 LEKDLHSGLIGPLIICKTG 169
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 1766-1902 1.85e-52

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 181.07  E-value: 1.85e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1766 MREFVLLFMTFDEKKSWYYEKKSRSSWR------LTSSEMKKSHEFHAINGMIY-SLPGLKMYEQEWVRLHLLNIGGSQD 1838
Cdd:cd04200    1 DKEFVLLFAVFDENKSWYLEDNIKRFCDnpekvdKDDEEFQESNKMHAINGYVFgNLPGLTMCAGDRVRWHLLGMGNEVD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88758619 1839 IHVVHFHGQTLLENGnkqHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLI 1902
Cdd:cd04200   81 VHSIHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1580-1753 4.63e-52

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 181.85  E-value: 4.63e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1580 RNYYIAAEEISWDYS----EFVQRETDIEDS----------DDIpeDTTYKKVVFRKYLDSTFTKRDPRGEYeehLGILG 1645
Cdd:cd04222    1 REYYIGIRETQWDYApsgkNLITNQTFDDDEhasvflkrgpDRI--GRVYKKAVYLQYTDDTYRTEIEKPVW---LGFLG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1646 PIIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSAC 1725
Cdd:cd04222   76 PILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANC 155

                        170       180
                 ....*....|....*....|....*...
gi 88758619 1726 RAWAYYSAVNPEKDIHSGLIGPLLICQK 1753
Cdd:cd04222  156 LTRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1580-1754 2.30e-51

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: 179.40  E-value: 2.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1580 RNYYIAAEEISWDYSEfVQRETDIEDSDDIPEDTT--YKKVVFRKYLDSTFTKRDPRGEYeehLGILGPIIRAEVDDVIQ 1657
Cdd:cd14452    1 RRYYIAAVEIGWDYIH-SDLGDPASEQRKKPKDIPqkYIKAVFVEYLDATFTVPKPRPAW---MGLLGPTIVAEVGDTVV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1658 VRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSAVNPE 1737
Cdd:cd14452   77 ITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPV 156

                        170
                 ....*....|....*..
gi 88758619 1738 KDIHSGLIGPLLICQKG 1754
Cdd:cd14452  157 KDVNSGLIGALLVCRMG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1582-1752 1.47e-50

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: 177.38  E-value: 1.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1582 YYIAAEEISWDYSEFVQRETDIE------DSDDIPEDTTYKKVVFRKYLDSTFTKR--DPRgeyEEHLGILGPIIRAEVD 1653
Cdd:cd14450    5 YFIAAEEVIWDYAPSIPENMDKRyrsqylDNFSNNIGKKYKKAVFTQYEDGSFTKRleNPR---PKEEGILGPVIRAQVR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1654 DVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSA 1733
Cdd:cd14450   82 DTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHSA 161

                        170
                 ....*....|....*....
gi 88758619 1734 VNPEKDIHSGLIGPLLICQ 1752
Cdd:cd14450  162 VDITRDIASGLIGPLLICK 180
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 1580-1754 1.65e-50

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


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 176.59  E-value: 1.65e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1580 RNYYIAAEEISWDYSefvqreTDIEDSDDIPEDTTYKKVVFRKYlDSTFTKRDPRGEYEehlGILGPIIRAEVDDVIQVR 1659
Cdd:cd04226    1 REYYIAAQNIDWDYT------PQSEELRLKRSEQSFKKIVYREY-EEGFKKEKPADLSS---GLLGPTLRAEVGDTLIVH 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1660 FKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSAVNPEKD 1739
Cdd:cd04226   71 FKNMADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRD 150

                        170
                 ....*....|....*
gi 88758619 1740 IHSGLIGPLLICQKG 1754
Cdd:cd04226  151 FNSGLIGALLICKKG 165
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 32-196 3.88e-50

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 175.94  E-value: 3.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   32 RQFYVAAQGISWSY--------RPEPTNSSLNLSVTsFKKIVYREY-EPYFKKEKPQSTISGLLGPTLYAEVGDIIKVHF 102
Cdd:cd14452    1 RRYYIAAVEIGWDYihsdlgdpASEQRKKPKDIPQK-YIKAVFVEYlDATFTVPKPRPAWMGLLGPTIVAEVGDTVVITF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  103 KNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDF 182
Cdd:cd14452   80 KNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVKDV 159

                        170
                 ....*....|....
gi 88758619  183 NSGLIGPLLICKKG 196
Cdd:cd14452  160 NSGLIGALLVCRMG 173
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 32-195 7.65e-50

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 175.30  E-value: 7.65e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   32 RQFYVAAQGISWSYRPEPTNSSLNLSVTS------------------FKKIVYREY-EPYFKKEKPQSTISGLLGPTLYA 92
Cdd:cd04222    1 REYYIGIRETQWDYAPSGKNLITNQTFDDdehasvflkrgpdrigrvYKKAVYLQYtDDTYRTEIEKPVWLGFLGPILKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   93 EVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIY 172
Cdd:cd04222   81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                        170       180
                 ....*....|....*....|...
gi 88758619  173 YSHENLIEDFNSGLIGPLLICKK 195
Cdd:cd04222  161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 351-527 1.76e-47

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: 168.75  E-value: 1.76e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  351 EYFIAAEEVIWDYAP----VIPANM--DKKYRSQHLDNFSNQIGKHYKKVMYTQYEDESFTKHTVNPnmKEDGILGPIIR 424
Cdd:cd04222    2 EYYIGIRETQWDYAPsgknLITNQTfdDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKP--VWLGFLGPILK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  425 AQVRDTLKIVFKNMASRPYSIYPHGVTfspYEDEVNSSF----TSGRNNTMiRAVQPGETYTYKWNILEFDEPTENDAQC 500
Cdd:cd04222   80 AEVGDVIVVHLKNFASRPYSLHPHGVF---YNKENEGALypdnTSGFEKAD-DAVPPGGSYTYTWTVPEEQAPTKADANC 155

                        170       180
                 ....*....|....*....|....*..
gi 88758619  501 LTRPYYSDVDIMRDIASGLIGLLLICK 527
Cdd:cd04222  156 LTRIYHSHIDAPKDIASGLIGPLIICK 182
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 352-527 2.19e-47

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: 168.03  E-value: 2.19e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  352 YFIAAEEVIWDYAPviPANMDKKYRSQHLDNFSNQ--------IGKHYKKVMYTQYEDESFTK-HTVNPNMKEDGILGPI 422
Cdd:cd04225    3 YYIAAEEVEWDYSP--QRTWEQELHNTHEESPGNAflnkgdkfIGSKYKKVVYREYTDDTFSVpKERTAEEEHLGILGPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  423 IRAQVRDTLKIVFKNMASRPYSIYPHGVTfspyedevnssfTSGrnnTMIRAVQPGETYTYKWNILEFDEPTENDAQCLT 502
Cdd:cd04225   81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK------------TDS---SWVAPTEPGETQTYTWKIPERSGPGVEDSNCIS 145

                        170       180
                 ....*....|....*....|....*
gi 88758619  503 RPYYSDVDIMRDIASGLIGLLLICK 527
Cdd:cd04225  146 WAYYSTVDQIKDLYSGLIGPLVICR 170
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1909-2060 5.96e-46

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: 162.52  E-value: 5.96e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1909 MPMGLSTGIiSDSQIKASEFLGY-WEPRLARLNnggSYNAWSveklAAEFASKPWIQVDMQKEVIITGIQTQGAKHYLKS 1987
Cdd:cd00057    1 EPLGMESGL-ADDQITASSSYSSgWEASRARLN---SDNAWT----PAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88758619 1988 CYTTEFYVAYSSNQINWQIFKGNStrNVMYFNGNSDASTIKENQFDPPIVARYIRISPTRAYNRPTLRLELQG 2060
Cdd:cd00057   73 EWVTSYKVQYSLDGETWTTYKDKG--EEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 352-528 6.17e-45

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 160.78  E-value: 6.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  352 YFIAAEEVIWDYAPVIPANMDKKYRSQHldnfsnqigKHYKKVMYTQYEDESFTKHTVNPNMKED-GILGPIIRAQVRDT 430
Cdd:cd14451    4 YYIAAEEEEWDYAGYGKSRLDKTQNERD---------TVFKKVVFRRYLDSTFSTPDIQGEYEEHlGILGPVIRAEVDDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  431 LKIVFKNMASRPYSIYPHGVTF------SPYEDEVNSSFTSGRnntmirAVQPGETYTYKWNILEFDEPTENDAQCLTRP 504
Cdd:cd14451   75 IQVFFKNLASRPYSLHAHGLSYekssegLSYDDESPDWFKKDD------AVQPNGTYTYVWYANPRSGPENNGSDCRTWA 148

                        170       180
                 ....*....|....*....|....
gi 88758619  505 YYSDVDIMRDIASGLIGLLLICKS 528
Cdd:cd14451  149 YYSAVNPEKDIHSGLIGPLLICRK 172
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 32-196 1.74e-44

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 159.62  E-value: 1.74e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   32 RQFYVAAQGISWSYRPePTNSSL----NLSVTSFKKIVYREY-EPYFKKEKPQSTIS---GLLGPTLYAEVGDIIKVHFK 103
Cdd:cd14451    2 RRYYIAAEEEEWDYAG-YGKSRLdktqNERDTVFKKVVFRRYlDSTFSTPDIQGEYEehlGILGPVIRAEVDDVIQVFFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  104 NKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFN 183
Cdd:cd14451   81 NLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKDIH 160

                        170
                 ....*....|...
gi 88758619  184 SGLIGPLLICKKG 196
Cdd:cd14451  161 SGLIGPLLICRKG 173
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1580-1754 3.16e-43

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: 156.04  E-value: 3.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1580 RNYYIAAEEISWDYS----------EFVQRETDIEDSDDIPEDTTYKKVVFRKYLDSTFTKRDPRgeyEEHLGILGPIIR 1649
Cdd:cd04229    1 RTYYIAAEEVDWDYApsgknkcclgDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPT---PAYLGILGPVIR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1650 AEVDDVIQVRFKN-LASRPYSLHAHGLSYEKSSEGKTYEDDSPewfkednaVQPNSSYTYVWHATERSGPESPGSACRAW 1728
Cdd:cd04229   78 AEVGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGTTDGAGDV--------VAPGETYTYRWIVPEDAGPGPGDPSSRLW 149

                        170       180
                 ....*....|....*....|....*.
gi 88758619 1729 AYYSAVNPEKDIHSGLIGPLLICQKG 1754
Cdd:cd04229  150 LYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 208-326 1.66e-41

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: 149.87  E-value: 1.66e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  208 DKQIVLLFAVFDE----------------------SKSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPE 265
Cdd:cd04200    1 DKEFVLLFAVFDEnkswylednikrfcdnpekvdkDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88758619  266 LFSIHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDI 326
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 ...
 351-527 2.25e-41

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


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 150.40  E-value: 2.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  351 EYFIAAEEVIWDYAPvipanmdkkyRSQHLDnfSNQIGKHYKKVMYTQYEdESFTKHtvNPNMKEDGILGPIIRAQVRDT 430
Cdd:cd04226    2 EYYIAAQNIDWDYTP----------QSEELR--LKRSEQSFKKIVYREYE-EGFKKE--KPADLSSGLLGPTLRAEVGDT 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  431 LKIVFKNMASRPYSIYPHGVTFSPYEDevNSSFTSGRN--NTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYSD 508
Cdd:cd04226   67 LIVHFKNMADKPLSIHPQGIAYGKKSE--GSLYSDNTSpvEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSH 144

                        170
                 ....*....|....*....
gi 88758619  509 VDIMRDIASGLIGLLLICK 527
Cdd:cd04226  145 VNMVRDFNSGLIGALLICK 163
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 547-684 3.70e-41

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: 148.86  E-value: 3.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  547 VFAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLgFCFDDTVQWHFCSVGTQNEILTIHF 626
Cdd:cd11016    7 LFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFV-ICLTDVAYWYVLSVGAQTDFLSVFF 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 88758619  627 TGHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRDVKC 684
Cdd:cd11016   86 SGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 33-194 4.86e-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: 150.03  E-value: 4.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   33 QFYVAAQGISWSYRPE-PTNSSL-----------NLSVTSFKKIVYREYEP-YFKK--EKPQSTISGLLGPTLYAEVGDI 97
Cdd:cd14450    4 EYFIAAEEVIWDYAPSiPENMDKryrsqyldnfsNNIGKKYKKAVFTQYEDgSFTKrlENPRPKEEGILGPVIRAQVRDT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   98 IKVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHEN 177
Cdd:cd14450   84 IKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHSAVD 163

                        170
                 ....*....|....*..
gi 88758619  178 LIEDFNSGLIGPLLICK 194
Cdd:cd14450  164 ITRDIASGLIGPLLICK 180
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 351-527 1.89e-40

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: 148.11  E-value: 1.89e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  351 EYFIAAEEVIWDYA-----PVIPANMDKKYRSQHLdnfsnqigKHYKKVMYTQYEDESFTKHTVNPNMKED-GILGPIIR 424
Cdd:cd04228    3 HYFIAAVEVLWDYGmqrpqHFLRARDPNRGRRKSV--------PQYKKVVFREYLDGSFTQPVYRGELDEHlGILGPYIR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  425 AQVRDTLKIVFKNMASRPYSIYPHGVTfspYEDEvnssftsGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRP 504
Cdd:cd04228   75 AEVEDNIMVTFKNLASRPYSFHSSLIS---YEED-------QRAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWA 144

                        170       180
                 ....*....|....*....|...
gi 88758619  505 YYSDVDIMRDIASGLIGLLLICK 527
Cdd:cd04228  145 YFSNVDLEKDLHSGLIGPLIICK 167
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 32-196 4.98e-39

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: 144.10  E-value: 4.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   32 RQFYVAAQGISWSYRP----------EPTNSSLNLSVTS------FKKIVYREY-EPYFKKEKPQSTISGLLGPTLYAEV 94
Cdd:cd04229    1 RTYYIAAEEVDWDYAPsgknkcclgdDLEVSTLDSQPGPytigstYTKARYREYtDNSFSTPKPTPAYLGILGPVIRAEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   95 GDIIKVHFKNKADK-PLSIHPQGIRYSKLSEGAsyldhtfpAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYY 173
Cdd:cd04229   81 GDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGT--------TDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYH 152

                        170       180
                 ....*....|....*....|...
gi 88758619  174 SHENLIEDFNSGLIGPLLICKKG 196
Cdd:cd04229  153 SHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1766-1902 2.31e-38

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: 140.79  E-value: 2.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1766 MREFVLLFMTFDEKKSWYYEKKSRSSWR------LTSSEMKKSHEFHAINGMIY-SLPGLKMYEQEWVRLHLLNIGGSQD 1838
Cdd:cd11018    1 VQEFALLFTIFDETKSWYFEENMRRNCRppchiqTQDPWFHINNKFHAINGYVAdTLPGLVMAQHQRIRWHLLNMGSDEE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88758619 1839 IHVVHFHGQTLLENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLI 1902
Cdd:cd11018   81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 351-527 5.72e-38

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: 140.88  E-value: 5.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  351 EYFIAAEEVIWDYAPVIPANMDKKYRSqhldnFSNQIGKHYKKVMYTQYEDESFTKHTVNPNMKedGILGPIIRAQVRDT 430
Cdd:cd14452    2 RYYIAAVEIGWDYIHSDLGDPASEQRK-----KPKDIPQKYIKAVFVEYLDATFTVPKPRPAWM--GLLGPTIVAEVGDT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  431 LKIVFKNMASRPYSIYPHGVTF------SPYEDEvnssfTSGRNNTMiRAVQPGETYTYKWNILEFDEPTENDAQCLTRP 504
Cdd:cd14452   75 VVITFKNLASQPYSLHAVGVSYwkasegAGYDDS-----TSQHEKED-DAVYPGGYHTYVWDISPKDGPTGSDPECLTYS 148

                        170       180
                 ....*....|....*....|...
gi 88758619  505 YYSDVDIMRDIASGLIGLLLICK 527
Cdd:cd14452  149 YSSQVDPVKDVNSGLIGALLVCR 171
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1906-2061 3.74e-37

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: 137.26  E-value: 3.74e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619    1906 DCRMPMGLStgiiSDSQIKASEflGYWEPRLARLNnGGSYNAWSveklAAEFASKPWIQVDMQKEVIITGIQTQGAKHYL 1985
Cdd:smart00231    1 PCNEPLGLE----SDSQITASS--SYWAAKIARLN-GGSDGGWC----PAKNDLPPWIQVDLGRLRTVTGVITGRRHGNG 69

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88758619    1986 KScytTEFYVAYSSNQINWQIFKGnstRNVMYFNGNSDASTIKENQFDPPIVARYIRISPTRAYNRPTLRLELQGC 2061
Cdd:smart00231   70 DW---VTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1582-1753 1.86e-36

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


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 136.98  E-value: 1.86e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1582 YYIAAEEISWDYSEFVQRETDIE-DSDDIPEDTT-----YKKVVFRKYLDSTFTKRDPRgeyEEHLGILGPIIRAEVDDV 1655
Cdd:cd04227    5 HYIAAEELDWDYAPLLSSTDDRElQSRYLPTGPQrigykYKKVAFVEYTDKTFKRREAK---QTEKGILGPLLKGEVGDQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1656 IQVRFKNLASRPYSLHAHGLS------YEKSSEGKTYEDDSPewfkednaVQPNSSYTYVWHATERSGPESPGSACRAWA 1729
Cdd:cd04227   82 IHIMFKNTASRPYNIYPHGLTsvrpmyRSRNPAGEKDLKTMP--------IGPGETFGYMWELTAEDGPTEEDPRCLTRL 153

                        170       180
                 ....*....|....*....|....
gi 88758619 1730 YYSAVNPEKDIHSGLIGPLLICQK 1753
Cdd:cd04227  154 YQSTVDPERDLASGLIGPLLICKK 177
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 34-195 2.89e-34

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: 130.43  E-value: 2.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   34 FYVAAQGISWSYRPEpTNSSLNLSVTS-------------FKKIVYREYE-PYFKKEKPQSTISGLLGPTLYAEVGDIIK 99
Cdd:cd04227    5 HYIAAEELDWDYAPL-LSSTDDRELQSrylptgpqrigykYKKVAFVEYTdKTFKRREAKQTEKGILGPLLKGEVGDQIH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  100 VHFKNKADKPLSIHPQGI------RYSKLSEGASYLdHTFPaekmddaVAPGREYTYEWSISEDSGPTHDDPPCLTHIYY 173
Cdd:cd04227   84 IMFKNTASRPYNIYPHGLtsvrpmYRSRNPAGEKDL-KTMP-------IGPGETFGYMWELTAEDGPTEEDPRCLTRLYQ 155

                        170       180
                 ....*....|....*....|..
gi 88758619  174 SHENLIEDFNSGLIGPLLICKK 195
Cdd:cd04227  156 STVDPERDLASGLIGPLLICKK 177
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 2065-2221 6.78e-34

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


Pssm-ID: 214572  Cd Length: 139  Bit Score: 128.01  E-value: 6.78e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619    2065 GCSTPLGMENgkieNKQITASSfkkswwgDYWEPFRARLNaQGRVNAWQAKANNNKQWLEIDLLKIKKITAIITQGCKSL 2144
Cdd:smart00231    1 PCNEPLGLES----DSQITASS-------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHGN 68

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88758619    2145 SSEMYvksYTIHYSEQGVEWKPYRLKSSMVdkiFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWNQSIALRLELFGC 2221
Cdd:smart00231   69 GDWVT---YKLEYSDDGVNWTTYKDGNSKV---FPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 32-195 2.90e-33

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: 127.58  E-value: 2.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   32 RQFYVAAQGISWSYRPE--------------PTNSSLN----LSVTSFKKIVYREY-EPYFKKEKPQST---ISGLLGPT 89
Cdd:cd04225    1 RTYYIAAEEVEWDYSPQrtweqelhntheesPGNAFLNkgdkFIGSKYKKVVYREYtDDTFSVPKERTAeeeHLGILGPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   90 LYAEVGDIIKVHFKNKADKPLSIHPQGIRysklsegasyLDHTFPAekmddAVAPGREYTYEWSISEDSGPTHDDPPCLT 169
Cdd:cd04225   81 IHAEVGEKVKIVFKNMASRPYSIHAHGVK----------TDSSWVA-----PTEPGETQTYTWKIPERSGPGVEDSNCIS 145

                        170       180
                 ....*....|....*....|....*.
gi 88758619  170 HIYYSHENLIEDFNSGLIGPLLICKK 195
Cdd:cd04225  146 WAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 351-525 5.34e-33

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: 126.76  E-value: 5.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  351 EYFIAAEEVIWDYAPvipANMDKKYRSQHLDNFS-------NQIGKHYKKVMYTQYEDESFTkhTVNPNMKEDGILGPII 423
Cdd:cd04229    2 TYYIAAEEVDWDYAP---SGKNKCCLGDDLEVSTldsqpgpYTIGSTYTKARYREYTDNSFS--TPKPTPAYLGILGPVI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  424 RAQVRDTLKIVFKN-MASRPYSIYPHGVTFSpyedEVNSSFTSGRNNtmirAVQPGETYTYKWNILEFDEPTENDAQCLT 502
Cdd:cd04229   77 RAEVGDTIKVVFKNnLDEFPVNMHPHGGLYS----KDNEGTTDGAGD----VVAPGETYTYRWIVPEDAGPGPGDPSSRL 148

                        170       180
                 ....*....|....*....|...
gi 88758619  503 RPYYSDVDIMRDIASGLIGLLLI 525
Cdd:cd04229  149 WLYHSHVDVFAHTNAGLVGPIIV 171
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 2081-2218 1.34e-31

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: 121.02  E-value: 1.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   2081 QITASSFkkswWGDYWEPfRARLNaqGRVN-AWQAKANNNKQWLEIDLLKIKKITAIITQGCKSLSSeMYVKSYTIHYSE 2159
Cdd:pfam00754    1 QITASSS----YSGEGPA-AAALD--GDPNtAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSN-GYVTSYKIEYSL 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88758619   2160 QGVEWKPYRlkssmvDKIFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWN--QSIALRLEL 2218
Cdd:pfam00754   73 DGENWTTVK------DEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNggNGIALRAEL 127
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 548-684 3.06e-31

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: 120.66  E-value: 3.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  548 FAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFT 627
Cdd:cd11022    8 FTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVHGIYFS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 88758619  628 GHSFIYGKRHEDTLTLFPMrgESVTVTM--DNVGTWMLTSMNSSPRSKKLRLKFRDVKC 684
Cdd:cd11022   88 GNTFLLQGTRRDTANLFPH--TSVTAIMqpDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 32-196 1.41e-30

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


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 119.61  E-value: 1.41e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   32 RQFYVAAQGISWSY---------RPEPTNSSLNLSVTSFKKIVYREY------EPYFKKEKPQSTisGLLGPTLYAEVGD 96
Cdd:cd04228    2 RHYFIAAVEVLWDYgmqrpqhflRARDPNRGRRKSVPQYKKVVFREYldgsftQPVYRGELDEHL--GILGPYIRAEVED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   97 IIKVHFKNKADKPLSIHPQGIRYSKLSEgasyldhtfpAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHE 176
Cdd:cd04228   80 NIMVTFKNLASRPYSFHSSLISYEEDQR----------AEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNV 149

                        170       180
                 ....*....|....*....|
gi 88758619  177 NLIEDFNSGLIGPLLICKKG 196
Cdd:cd04228  150 DLEKDLHSGLIGPLIICKTG 169
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 548-669 2.01e-30

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: 117.96  E-value: 2.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  548 FAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFT 627
Cdd:cd11021    8 FSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHSAFFH 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 88758619  628 GHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSS 669
Cdd:cd11021   88 GQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVND 129
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1767-1900 1.50e-25

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: 104.09  E-value: 1.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1767 REFVLLFMTFDEKKSWYYEKKSRSSWRLTSSEMKKSHEF------HAINGMIY-SLPGLKMYEQEWVRLHLLNIGGSQDI 1839
Cdd:cd11021    2 REFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFqesnkmHSINGYTFgNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88758619 1840 HVVHFHGQTLLENGnkqHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPF 1900
Cdd:cd11021   82 HSAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFY 139
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 547-663 2.36e-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: 103.79  E-value: 2.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  547 VFAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHF 626
Cdd:cd11012    7 LFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHTAHF 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 88758619  627 TGHSFIY---GKRHEDTLTLFPMRGESVTVTMDNVGTWML 663
Cdd:cd11012   87 HGHSFDYkhrGVYRSDVFDLFPGTFQTVEMIPRTPGTWLL 126
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1768-1903 3.98e-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: 103.02  E-value: 3.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1768 EFVLLFMTFDEKKSWYYEKKSRSSWRLTSSEMKKSHEF------HAINGMIY-SLPGLKMYEQEWVRLHLLNIGGSQDIH 1840
Cdd:cd11012    3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFiesnkmHAINGKVFgNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88758619 1841 VVHFHGQTLLENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLIM 1903
Cdd:cd11012   83 TAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1922-2058 1.11e-24

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: 101.37  E-value: 1.11e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   1922 QIKASEFLGYWEPRLARLNNGGSyNAWSveklAAEFASKPWIQVDMQKEVIITGIQTQGAKHyLKSCYTTEFYVAYSSNQ 2001
Cdd:pfam00754    1 QITASSSYSGEGPAAAALDGDPN-TAWS----AWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 88758619   2002 INWQIFKGNSTrnvmyfNGNSDASTIKENQFDPPIVARYIRISPTRA--YNRPTLRLEL 2058
Cdd:pfam00754   75 ENWTTVKDEKI------PGNNDNNTPVTNTFDPPIKARYVRIVPTSWngGNGIALRAEL 127
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 230-326 1.37e-23

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: 98.70  E-value: 1.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  230 LMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIIS 309
Cdd:cd11021   45 KMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLS 124

                         90
                 ....*....|....*..
gi 88758619  310 SLTPKHLQAGMQAYIDI 326
Cdd:cd11021  125 CQVNDHLKAGMQAFYEV 141
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 548-663 9.59e-22

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


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 93.41  E-value: 9.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  548 FAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFT 627
Cdd:cd11018    8 FTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHSVHFH 87

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 88758619  628 GHSFIYGKRHEDTL---TLFPMRGESVTVTMDNVGTWML 663
Cdd:cd11018   88 GLPFTVRAKKEYRMgvyNLYPGVFGTVEMRPSTAGIWLV 126
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1767-1902 2.91e-21

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 91.51  E-value: 2.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1767 REFVLLFMTFDEKKSWYYEKKSRSSW-RLTSSEMKKshEFHAINGMIY-SLPGLKMYEQEWVRLHLLNIGGSQDIHVVHF 1844
Cdd:cd11015    2 QAFVLLFAVFDEGKSWYSEVGERKSRdKFKRADSRK--EFHTINGYINaSLPGLKICQRKPVIWHVIGMGTAPEVHSIFF 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 88758619 1845 HGQTLLEngnKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLI 1902
Cdd:cd11015   80 EGHTFLV---RTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 209-326 8.05e-21

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


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 90.35  E-value: 8.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  209 KQIVLLFAVFDE---------------SKSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNG 273
Cdd:cd11015    2 QAFVLLFAVFDEgkswysevgerksrdKFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFFEG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 88758619  274 QVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDI 326
Cdd:cd11015   82 HTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1767-1902 7.67e-19

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: 84.20  E-value: 7.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1767 REFVLLFMTFDEKkswyyekksrsswrltssEMKKSHEFHAINGMIY-SLPGLKMYEQEWVRLHLLNIGGSQDIHVVHFH 1845
Cdd:cd11023    2 QEFIENSSIFLDL------------------NVEEAGLMHSINGYVFgNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWH 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 88758619 1846 GQTLLENGNKQHQlgVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLI 1902
Cdd:cd11023   64 GQTVEADKSRRTD--VAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1767-1897 3.77e-18

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 82.21  E-value: 3.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1767 REFVLLFMTFDEKKSWYyekksrsswrltSSEMKKSHEFHAINGMIY-SLPGLKMYEQEWVRLHLLNIGGSQDIHVVHFH 1845
Cdd:cd14453    2 KEYVLMFGVFDENKSWY------------KQNASVDSVKYTINGYTNgTLPDVSICAYDHVSWHLLGMSSEPELFSVHFN 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 88758619 1846 GQTLLENGNKQHQLGvwpLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQ 1897
Cdd:cd14453   70 GQVLEQNGHKVSAVG---LVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMY 118
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1767-1896 1.27e-17

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 81.76  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1767 REFVLLFMTFDEKKSWYYEKKSR------SSWRLTSSEMKKSHEFHAINGMIYS-LPGLKMYEQEWVRLHLLNIGGSQDI 1839
Cdd:cd11022    2 KEFFLLFTVFDENESWYLDENIQqftldpRSVDKEDEDFQESNKMHSINGYMYGnQPGLDMCKGDTVSWHLFGLGTETDV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 88758619 1840 HVVHFHGQTLLENGNKQHQLGvwpLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGM 1896
Cdd:cd11022   82 HGIYFSGNTFLLQGTRRDTAN---LFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGM 135
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 208-329 3.49e-14

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: 71.74  E-value: 3.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  208 DKQIVLLFAVFDESKSWSQSSSL----------------------MYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPE 265
Cdd:cd11022    1 DKEFFLLFTVFDENESWYLDENIqqftldprsvdkededfqesnkMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88758619  266 LFSIHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDIKNC 329
Cdd:cd11022   81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 543-666 8.32e-14

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 69.89  E-value: 8.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  543 EQQAV--FAVFDENKSWYledninkfcenpdevkRDDPKfyESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNE 620
Cdd:cd14453    1 YKEYVlmFGVFDENKSWY----------------KQNAS--VDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 88758619  621 ILTIHFTGHSFIYGKRHEDTLTLfpMRGESVTVTMDNV--GTWMLTSM 666
Cdd:cd14453   63 LFSVHFNGQVLEQNGHKVSAVGL--VSGSSTTASMTVVhtGRWLISSL 108
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 84-193 8.78e-14

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 69.62  E-value: 8.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   84 GLLGPTLYAEVGDIIKVHFKNKAD-KPLSIHPQGIRYsklsEGASylDHTFPAEKMDDAVAPGREYTYEWSISEDSGpth 162
Cdd:cd04206   27 QFPGPTIRVKEGDTVEVTVTNNLPnEPTSIHWHGLRQ----PGTN--DGDGVAGLTQCPIPPGESFTYRFTVDDQAG--- 97

                         90       100       110
                 ....*....|....*....|....*....|.
gi 88758619  163 ddppclTHIYYSHENLieDFNSGLIGPLLIC 193
Cdd:cd04206   98 ------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1630-1751 3.22e-13

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 68.08  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1630 KRDPRGEYEEHLGILGPIIRAEVDDVIQVRFKN-LASRPYSLHAHGLSYEKSSEGktyedDSPEWFKEDnAVQPNSSYTY 1708
Cdd:cd04206   15 DGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDG-----DGVAGLTQC-PIPPGESFTY 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 88758619 1709 VWHATERSGpespgsacrAWAYYSAVNPEKDihSGLIGPLLIC 1751
Cdd:cd04206   89 RFTVDDQAG---------TFWYHSHVGGQRA--DGLYGPLIVE 120
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 547-671 5.87e-13

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: 68.01  E-value: 5.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  547 VFAVFDENKSWYLEDNINKfceNPDEVKRDD--PKFYesnimsTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTI 624
Cdd:cd11015    7 LFAVFDEGKSWYSEVGERK---SRDKFKRADsrKEFH------TINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 88758619  625 HFTGHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPR 671
Cdd:cd11015   78 FFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQ 124
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 87-192 1.57e-12

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 66.14  E-value: 1.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   87 GPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYsklsegaSYLDHTFPAEkmddaVAPGREYTYEWsISEDSGpthddpp 166
Cdd:cd11024   32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHD-------AAMDGTGLGP-----IMPGESFTYEF-VAEPAG------- 91

                         90       100
                 ....*....|....*....|....*..
gi 88758619  167 clTHIYYSH-ENLIEDFNSGLIGPLLI 192
Cdd:cd11024   92 --THLYHCHvQPLKEHIAMGLYGAFIV 116
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 232-322 4.61e-12

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: 65.67  E-value: 4.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  232 YTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVL---EQNHHKVSAITLVSATSTTANMTVGPEGKWII 308
Cdd:cd11018   47 HAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHSVHFHGLPFtvrAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLV 126

                         90
                 ....*....|....
gi 88758619  309 SSLTPKHLQAGMQA 322
Cdd:cd11018  127 ECTVGEHLLAGMSA 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 208-320 5.04e-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: 64.55  E-value: 5.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  208 DKQIVLLFAVFDESKSWSQSssLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKVSAI- 286
Cdd:cd11023    1 DQEFIENSSIFLDLNVEEAG--LMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRTDVa 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 88758619  287 TLVSATSTTANMTVGPEGKWIISSLTPKHLQAGM 320
Cdd:cd11023   79 ELMPASMRVADMTAADVGTWLLHCHVHDHYMAGM 112
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 548-665 7.45e-12

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: 64.89  E-value: 7.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  548 FAVFDENKSWYLEDNINKFCEnpdEVKRDDPKFYESNIMSTINGyVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFT 627
Cdd:cd14455    8 FMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAING-IIYNLKGLRMYTNELVRWHLINMGGPKDLHVVHFH 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 88758619  628 GHSFIYGKRHEDTLTLFP-MRGESVTVTM--DNVGTWMLTS 665
Cdd:cd14455   84 GQTFTEKGLKDHQLGVYPlLPGSFATLEMkpSKPGLWLLET 124
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 76-192 6.15e-11

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: 61.51  E-value: 6.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   76 EKPQSTISGLL-GPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRysklSEGASYLDHTfpAEKMDDAVAPGREYTYEWSI 154
Cdd:cd13857   18 VRPMLVINGQFpGPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGT--AGITQCPIPPGGSFTYNFTV 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 88758619  155 SEDSGpthddppclTHIYYSH-ENLIEDfnsGLIGPLLI 192
Cdd:cd13857   92 DGQYG---------TYWYHSHySTQYAD---GLVGPLIV 118
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 416-526 8.96e-11

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 61.15  E-value: 8.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  416 DGILGPIIRAQVRDTLKIVFKN-MASRPYSIYPHGVTF--SPYEDEVNSSFTSgrnntmirAVQPGETYTYKWNIlefde 492
Cdd:cd04206   26 GQFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQpgTNDGDGVAGLTQC--------PIPPGESFTYRFTV----- 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 88758619  493 ptenDAQCLTRPYYSDVDImrDIASGLIGLLLIC 526
Cdd:cd04206   93 ----DDQAGTFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 84-192 6.00e-10

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: 58.79  E-value: 6.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   84 GLLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLdhTFPaekmddAVAPGREYTYEWSIsEDSGpthd 163
Cdd:cd13861   28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGL--TQP------PVPPGESFTYEFTP-PDAG---- 94

                         90       100
                 ....*....|....*....|....*....
gi 88758619  164 dppclTHIYYSHENLIEDFNSGLIGPLLI 192
Cdd:cd13861   95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1770-1902 7.83e-10

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: 59.11  E-value: 7.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1770 VLLFMTFDEKKSWYYEK------KSRSSWRLTSSEMKKSHEFHAINGMIYSLPGLKMYEQEWVRLHLLNIGGSQDIHVVH 1843
Cdd:cd11016    5 SLLFSVFDENNSWYLKEnihrftQTPAGVNDTDPDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDFLSVF 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 88758619 1844 FHGQTLLENGNKQHQLgvwPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLI 1902
Cdd:cd11016   85 FSGNTFKHQMVYEDVL---TLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTV 140
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 208-329 5.81e-09

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


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 56.80  E-value: 5.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  208 DKQIVLLFAVFDESKS----------------------WSQSSSLMYTVNGYVNGTMpDITVCAHDHISWHLLGMSSGPE 265
Cdd:cd11016    1 DKDWSLLFSVFDENNSwylkenihrftqtpagvndtdpDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88758619  266 LFSIHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDIKNC 329
Cdd:cd11016   80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 85-192 1.05e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 59.95  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   85 LLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYsklsegasyldhtfPAEkMD----DAVAPGREYTYEWSIsedsgp 160
Cdd:COG2132   42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRV--------------PNA-MDgvpgDPIAPGETFTYEFPV------ 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 88758619  161 thDDPPClTHIYYSHENLIEDFN--SGLIGPLLI 192
Cdd:COG2132  101 --PQPAG-TYWYHPHTHGSTAEQvyRGLAGALIV 131
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 81-192 1.58e-08

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: 54.56  E-value: 1.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619     81 TISG-LLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSK--LSEGASYLDHtfpaekmdDAVAPGREYTYEWSISED 157
Cdd:pfam07732   19 GVNGqFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGtpWMDGVPGVTQ--------CPIPPGQSFTYRFQVKQQ 90

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 88758619    158 SGpthddppclTHIYYSHENLIEdfNSGLIGPLLI 192
Cdd:pfam07732   91 AG---------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 550-663 3.76e-08

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 53.77  E-value: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  550 VFDENKSWYLEDNINkfcenpdevkrddpkfyESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFTGH 629
Cdd:cd11023    3 EFIENSSIFLDLNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQ 65

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 88758619  630 SFIYGK-RHEDTLTLFPMRGESVTVTMDNVGTWML 663
Cdd:cd11023   66 TVEADKsRRTDVAELMPASMRVADMTAADVGTWLL 100
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1643-1867 6.89e-08

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


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 57.25  E-value: 6.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1643 ILGPIIRAEVDDVIQVRFKNLASRPYSLHAHGL--SYEkssegktyEDDSPEwfkedNAVQPNSSYTYVWHATERSG--- 1717
Cdd:COG2132   42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLrvPNA--------MDGVPG-----DPIAPGETFTYEFPVPQPAGtyw 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1718 --PESPGSacrawayySAVNpekdIHSGLIGPLLIcqkgilH-KDSNMPMDMREFVLLF--MTFDEKKSWYYekksrssw 1792
Cdd:COG2132  109 yhPHTHGS--------TAEQ----VYRGLAGALIV------EdPEEDLPRYDRDIPLVLqdWRLDDDGQLLY-------- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1793 RLTSSEMKKSHEFHAINGMIysLPGLKMYEQEWVRLHLLNIGGS----------QDIHVVHFHGQTLlengNKQHQLGVW 1862
Cdd:COG2132  163 PMDAAMGGRLGDTLLVNGRP--NPTLEVRPGERVRLRLLNASNAriyrlalsdgRPFTVIATDGGLL----PAPVEVDEL 236


                 ....*
gi 88758619 1863 PLLPG 1867
Cdd:COG2132  237 LLAPG 241
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 62-192 7.51e-08

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 53.42  E-value: 7.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   62 KKIVYREYEPYFKKEKPQstisgLLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASyldhtFPAEkmddA 141
Cdd:cd14449    9 EKLTDDAWGYGLKGGVAT-----VPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG-----MNAS----I 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 88758619  142 VAPGREYTYEW----SISEDSGPTHDDPPCLTHiYYSH----ENLIEDFNSGLIGPLLI 192
Cdd:cd14449   75 VAPGDTRIYTWrthgGYRRADGSWAEGTAGYWH-YHDHvfgtEHGTEGLSRGLYGALIV 132
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1772-1901 2.25e-07

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: 52.18  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1772 LFMTFDEKKSWYYEKKSRSSWRLTSSEMKKSHEF------HAINGMIY-SLPGLKMYEQEWVRLHLLNIGGSQDIHVVHF 1844
Cdd:cd14454    7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFyksnimPTINGYAYeSSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 88758619 1845 HGQTLLENGNKQHQLGVWPLlpgSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFL 1901
Cdd:cd14454   87 SGHTFRYKGKHEDTLNLFPM---SGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFT 140
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 231-322 2.79e-07

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: 51.79  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  231 MYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNH---HKVSAITLVSATSTTANMTVGPEGKWI 307
Cdd:cd11012   46 MHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHTAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWL 125

                         90
                 ....*....|....*
gi 88758619  308 ISSLTPKHLQAGMQA 322
Cdd:cd11012  126 LHCHVTDHIHAGMET 140
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1645-1750 3.51e-07

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 51.50  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1645 GPIIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTyeddspewfKEDNAVQPNSSYTYVW--HATER--SGPES 1720
Cdd:cd14449   29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG---------MNASIVAPGDTRIYTWrtHGGYRraDGSWA 99

                         90       100       110
                 ....*....|....*....|....*....|....
gi 88758619 1721 PGSAcRAWAYYSAV----NPEKDIHSGLIGPLLI 1750
Cdd:cd14449  100 EGTA-GYWHYHDHVfgteHGTEGLSRGLYGALIV 132
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1645-1750 8.50e-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: 49.96  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1645 GPIIRAEVDDVIQVRFKNLASRPYSLHAHGLSyekssegKTYEDDSpewFKEDnaVQPNSSYTYVWHATErsgpesPGsa 1724
Cdd:cd11024   32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIH-------DAAMDGT---GLGP--IMPGESFTYEFVAEP------AG-- 91

                         90       100
                 ....*....|....*....|....*..
gi 88758619 1725 crAWAYYSAVNPEKD-IHSGLIGPLLI 1750
Cdd:cd11024   92 --THLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 405-525 1.15e-06

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 49.50  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  405 TKHTVNPNMKEDG------ILGPIIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDEVnSSFTSgrnntmiRAVQPG 478
Cdd:cd13860   10 VKWEIAPGVKVEAwgyngsVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV-PGITQ-------PPIQPG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 88758619  479 ETYTYkwnilEFDeptendaqcLTRP----YYSDVDIMRDIASGLIGLLLI 525
Cdd:cd13860   82 ETFTY-----EFT---------AKQAgtymYHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 87-192 1.40e-06

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


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 49.12  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   87 GPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRysklsegasyldhtFPAEkMD-------DAVAPGREYTYEWSIsEDSG 159
Cdd:cd13860   31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLP--------------VPNG-MDgvpgitqPPIQPGETFTYEFTA-KQAG 94

                         90       100       110
                 ....*....|....*....|....*....|...
gi 88758619  160 pthddppclTHIYYSHENLIEDFNSGLIGPLLI 192
Cdd:cd13860   95 ---------TYMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 420-485 1.73e-06

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 49.01  E-value: 1.73e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88758619  420 GPIIRAQVRDTLKIVFKNMASRPYSIYPHGVTfspyedEVNSSFTSGRNNTMIRAVQPGETYTYKW 485
Cdd:cd13859   31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVL------QMGSWKMDGVPGVTQPAIEPGESFTYKF 90
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 420-525 2.35e-06

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 48.42  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  420 GPIIRAQVRDTLKIVFKNMASRPYSIYPHGVtFSPYEDevnssftsGRNNTMIRavqPGETYTYKWnilefdeptenDAQ 499
Cdd:cd11024   32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGI-HDAAMD--------GTGLGPIM---PGESFTYEF-----------VAE 88

                         90       100
                 ....*....|....*....|....*...
gi 88758619  500 CL-TRPYYSDV-DIMRDIASGLIGLLLI 525
Cdd:cd11024   89 PAgTHLYHCHVqPLKEHIAMGLYGAFIV 116
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 420-485 2.63e-06

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 48.80  E-value: 2.63e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88758619  420 GPIIRAQVRDTLKIVFKNMASRPYSIYPHGVTFspyedEVNSSFTsGRNNTmirAVQPGETYTYKW 485
Cdd:cd14449   29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDY-----TTASDGT-GMNAS---IVAPGDTRIYTW 85
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 230-321 7.48e-06

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: 47.94  E-value: 7.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  230 LMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIIS 309
Cdd:cd14454   45 IMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLG 124

                         90
                 ....*....|..
gi 88758619  310 SLTPKHLQAGMQ 321
Cdd:cd14454  125 SFGSSKKSKGLR 136
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 81-192 1.54e-05

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


Pssm-ID: 259917 [Multi-domain]  Cd Length: 116  Bit Score: 46.12  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   81 TISGLL-GPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLdhTFPaekmddAVAPGREYTYEWSISEdSG 159
Cdd:cd13848   23 TVNGQVpGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDMDGVPGL--SFP------GIKPGETFTYRFPVRQ-SG 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 88758619  160 pthddppclTHIYYSHENLIEdfNSGLIGPLLI 192
Cdd:cd13848   94 ---------TYWYHSHSGLQE--QTGLYGPIII 115
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 209-322 2.26e-05

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: 46.40  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  209 KQIVLLFAVFDE-------------------SKSWSQSSSLMYTVNGYVNgTMPDITVCAHDHISWHLLGMSSGPELFSI 269
Cdd:cd14455    2 REFVLLFMTFDEekswyyeknrkrtcrenrvKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 88758619  270 HFNGQVLEQN---HHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQA 322
Cdd:cd14455   81 HFHGQTFTEKglkDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQT 136
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 1642-1750 5.19e-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: 44.53  E-value: 5.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1642 GILGPIIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPewfkednaVQPNSSYTYvwhateRSGPESP 1721
Cdd:cd13861   28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGLTQPP--------VPPGESFTY------EFTPPDA 93

                         90       100
                 ....*....|....*....|....*....
gi 88758619 1722 GSACrawaYYSAVNPEKDIHSGLIGPLLI 1750
Cdd:cd13861   94 GTYW----YHPHVGSQEQLDRGLYGPLIV 118
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1624-1717 1.53e-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: 43.44  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1624 LDSTFTKRDPRGEYEEHLGIL------GPIIRAEVDDVIQVRFKNLASRPYSLHAHGLsyekSSEGKTYEDDSP---EWf 1694
Cdd:cd13850    1 FTLTVTEGSPDGDGGEREVILingqfpGPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPWSDGVPgvtQW- 75

                         90       100
                 ....*....|....*....|...
gi 88758619 1695 kednAVQPNSSYTYVWHATERSG 1717
Cdd:cd13850   76 ----PIQPGGSFTYRWKAEDQYG 94
YjbI COG1357
Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];
1234-1421 1.69e-04

Uncharacterized conserved protein YjbI, contains pentapeptide repeats [Function unknown];


Pssm-ID: 440968 [Multi-domain]  Cd Length: 178  Bit Score: 44.55  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1234 DLSHTTLS-PDLSHTTLS-LDLSQTNLSPELSQTNLSPAlgqmplspDLSHTTLS-LDFSQTNLSP-ELSHMTLS-PELS 1308
Cdd:COG1357    1 DLSGADLSgADLSGADLSgADLSGANLSGALSGANLSGA--------NLSGANLTgANLSGADLSGaDLSGANLSgADLS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1309 QTNLSPAlgqmpispDLSHTTLsLDFSQTNLSP-ELSQTNLSPAlgqmplspDPSHTTLS-LDLSQTNLS-PELSQTNLS 1385
Cdd:COG1357   73 GANLTGA--------DLSGANL-ANLSGANLSGaNLSGANLRGA--------NLSGANLSgADLSGADLSgANLSGADLS 135

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 88758619 1386 P-DLSEmplfADLSQIpltpDLDQMTLSP-DLGETDLS 1421
Cdd:COG1357  136 GaNLSG----ANLSGA----DLSGADLSGaNLSGANLS 165
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 408-487 1.92e-04

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 43.00  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619    408 TVNpnmkeDGILGPIIRAQVRDTLKIVFKNMASRPYSIYPHG--VTFSPYEDEVNssftsGRNNTMIravQPGETYTYKW 485
Cdd:pfam07732   19 GVN-----GQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGlqQRGTPWMDGVP-----GVTQCPI---PPGQSFTYRF 85


                   ..
gi 88758619    486 NI 487
Cdd:pfam07732   86 QV 87
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 420-487 3.02e-04

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 42.63  E-value: 3.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  420 GPIIRAQVRDTLKIVFKNMASRPYSIYPHGVTF--SPYEDEvnssfTSGRNNTMIravQPGETYTYKWNI 487
Cdd:cd13857   30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQngTNWMDG-----TAGITQCPI---PPGGSFTYNFTV 91
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 1645-1750 3.20e-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: 42.25  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1645 GPIIRAEVDDVIQVRFKNLASRPYSLHAHGLsYEkssEGKTYEDDSPEWfkEDNAVQPNSSYTYVWHATERSGPespgsa 1724
Cdd:cd13857   30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGL-FQ---NGTNWMDGTAGI--TQCPIPPGGSFTYNFTVDGQYGT------ 97

                         90       100
                 ....*....|....*....|....*...
gi 88758619 1725 crAW--AYYSAVNPEkdihsGLIGPLLI 1750
Cdd:cd13857   98 --YWyhSHYSTQYAD-----GLVGPLIV 118
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 1645-1750 3.26e-04

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: 42.47  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1645 GPIIRA-EVDDVIqVRFKNLASRPYSLHAHGLsYEKSSegkTYEDDSPEWFKEdnAVQPNSSYTYVWHAtersgpESPGS 1723
Cdd:cd13859   31 GPLIHVkEGDDLV-VHVTNNTTLPHTIHWHGV-LQMGS---WKMDGVPGVTQP--AIEPGESFTYKFKA------ERPGT 97

                         90       100
                 ....*....|....*....|....*...
gi 88758619 1724 acrAWaYYSAVN-PEKDIHSGLIGPLLI 1750
Cdd:cd13859   98 ---LW-YHCHVNvNEHVGMRGMWGPLIV 121
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 75-159 3.51e-04

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


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 42.25  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   75 KEKPQSTISGLL-GPTLYAEVGDIIKVHFKNKADKPLSIHPQGIR--YSKLSEGASYLDHTfPAEkmddavaPGREYTYE 151
Cdd:cd13849   15 STKSILTVNGQFpGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRqlRSGWADGPAYITQC-PIQ-------PGQSYTYR 86


                 ....*...
gi 88758619  152 WSISEDSG 159
Cdd:cd13849   87 FTVTGQEG 94
PLN02191 PLN02191
L-ascorbate oxidase
 75-192 3.87e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 45.39  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619    75 KEKPQSTISGLL-GPTLYAEVGDIIKVHFKNK-ADKPLSIHPQGIRY--SKLSEGASYLDHTfpaekmddAVAPGREYTY 150
Cdd:PLN02191   40 KEGAVMTVNGQFpGPTIDAVAGDTIVVHLTNKlTTEGLVIHWHGIRQkgSPWADGAAGVTQC--------AINPGETFTY 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 88758619   151 EWSIsEDSGpthddppclTHIYYSHENLIEdfNSGLIGPLLI 192
Cdd:PLN02191  112 KFTV-EKPG---------THFYHGHYGMQR--SAGLYGSLIV 141
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 87-192 6.16e-04

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 41.84  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   87 GPTLYAEVGDIIKVHFKNK-ADKPLSIHPQGIR--YSKLSEGASYLDHTfpaekmddAVAPGREYTYEWSISEdSGpthd 163
Cdd:cd13854   33 GPLIEANWGDTIEVTVINKlQDNGTSIHWHGIRqlNTNWQDGVPGVTEC--------PIAPGDTRTYRFRATQ-YG---- 99

                         90       100
                 ....*....|....*....|....*....
gi 88758619  164 dppclTHIYYSHENLieDFNSGLIGPLLI 192
Cdd:cd13854  100 -----TSWYHSHYSA--QYGDGVVGPIVI 121
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 75-192 9.89e-04

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 44.36  E-value: 9.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619     75 KEKPQSTISGLL-GPTLYAEVGDIIKVHFKNK-ADKPLSIHPQGIRysklSEGASYLDHTfpAEKMDDAVAPGREYTYEW 152
Cdd:TIGR03388   18 FEKLVIGINGQFpGPTIRAQAGDTIVVELTNKlHTEGVVIHWHGIR----QIGTPWADGT--AGVTQCAINPGETFIYNF 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 88758619    153 SIsedsgpthDDPPclTHIYYSHENLIEdfNSGLIGPLLI 192
Cdd:TIGR03388   92 VV--------DRPG--TYFYHGHYGMQR--SAGLYGSLIV 119
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1794-1906 1.03e-03

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 41.27  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   1794 LTSSEMKKSheFHAINGMIYSL--PGLKMYEQEWVRLHLLNigGSQDIHVVHFHGQT--LLENGNKQHQL---------- 1859
Cdd:pfam07731   12 ITSGNFRRN--DWAINGLLFPPntNVITLPYGTVVEWVLQN--TTTGVHPFHLHGHSfqVLGRGGGPWPEedpktynlvd 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 88758619   1860 GVW----PLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLIMDRD 1906
Cdd:pfam07731   88 PVRrdtvQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 86-175 1.19e-03

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


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 40.73  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   86 LGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGasyldHtfPAekmdDAVAPGREYTYEWSISEDSGpthddp 165
Cdd:cd13852   23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG-----H--PR----YAIDPGETYVYEFEVLNRAG------ 85

                         90
                 ....*....|
gi 88758619  166 pclTHIYYSH 175
Cdd:cd13852   86 ---TYWYHPH 92
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1794-1900 1.27e-03

The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 41.35  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1794 LTSSEMKKSHEFHAINGM--IYSLPGLKMYEQEWVRLHLLNIGGSQdiHVVHFHG---QTLLENGNkqhqLGVWP----L 1864
Cdd:cd13909   25 MSMRELIQLGQFWAFNGVagRPDDPLLEARRGETVRIEMVNNTGFP--HGMHLHGhhfRAILPNGA----LGPWRdtllM 98

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 88758619 1865 LPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPF 1900
Cdd:cd13909   99 DRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWF 134
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 88-192 1.28e-03

The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259920 [Multi-domain]  Cd Length: 121  Bit Score: 40.71  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   88 PTLYAEVGDIIKVHFKNK-ADKPLSIHPQGIryskLSEGASYldhtfpaekMDDAV-------APGREYTYEWSISEDSG 159
Cdd:cd13851   32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGL----FQNGTNY---------MDGPVgvtqcpiPPGQSFTYEFTVDTQVG 98

                         90       100       110
                 ....*....|....*....|....*....|...
gi 88758619  160 pthddppclTHIYYSHENliEDFNSGLIGPLLI 192
Cdd:cd13851   99 ---------TYWYHSHDG--GQYPDGLRGPFII 120
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 1213-1389 3.00e-03

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 42.96  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1213 LSPELIQRNLSPALGQMPISPDLSHTTLSPDLSHTTLSLDL-SQTNLSPELSQTNLSPalGQMPLSPDLSHTTLSLD-FS 1290
Cdd:COG5422   32 LPPRRLQRKLNPISIRNGADNDIINSESKESFGKYALGHQIfSSFSSSPKLFQRRNSA--GPITHSPSATSSTSSLNsND 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619 1291 QTNLSPelSHMTLSPELSQTNLSPALGQMPISP-DLSHTTLSLDFSQTNLSPELSQTNLSPALGQMPLSPDPSHTTLSLD 1369
Cdd:COG5422  110 GDQFSP--ASDSLSFNPSSTQSRKDSGPGDGSPvQKRKNPLLPSSSTHGTHPPIVFTDNNGSHAGAPNARSRKEIPSLGS 187

                        170       180
                 ....*....|....*....|
gi 88758619 1370 LSQTNLSPELSQTNLSPDLS 1389
Cdd:COG5422  188 QSMQLPSPHFRQKFSSSDTS 207
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 389-525 3.30e-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: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619  389 KHYK-KVMYTQYEDESFTKHTVNPNmkeDGILGPIIRAQVRDTLKIVFKN-MASRPYSIYPHGV--TFSPYEDEVNSSFT 464
Cdd:cd13845    1 RHYKwKVEYMFWAPDCVEKLVIGIN---GQFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGIrqRGTPWADGTASVSQ 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88758619  465 SgrnntmirAVQPGETYTYKWNIlefDEPTendaqclTRPYYSDVDIMRdiASGLIGLLLI 525
Cdd:cd13845   78 C--------PINPGETFTYQFVV---DRPG-------TYFYHGHYGMQR--SAGLYGSLIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1643-1717 3.38e-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: 39.54  E-value: 3.38e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88758619   1643 ILGPIIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSegktYEDDSPEWfkEDNAVQPNSSYTYVWHATERSG 1717
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTP----WMDGVPGV--TQCPIPPGQSFTYRFQVKQQAG 92
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1807-1883 4.31e-03

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 39.18  E-value: 4.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88758619 1807 AINGMIyslPG--LKMYEQEWVRLHLLNIGGsqDIHVVHFHGQtlleNGNKQHQLGVWPLLPGSFKTLEMKASKPGWWL 1883
Cdd:cd11024   25 TYNGTV---PGptLRATEGDLVRIHFINTGD--HPHTIHFHGI----HDAAMDGTGLGPIMPGESFTYEFVAEPAGTHL 94
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 548-670 5.31e-03

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: 39.61  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619    548 FAVFDENKSWYlEDNINKFCENPDEVKRDDPKFyeSNIMS--TINGYVPESITTLGFCFDDTVQWHFCSVGTQNEiLTIH 625
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDF--PPVPDavLINGKDGASLATLTVTPGKTYRLRIINVALDDS-LNFS 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 88758619    626 FTGHSFIY----GKRHE----DTLTLFPmrGE--SVTVTMDN-VGT-WMLTSMNSSP 670
Cdd:pfam00394   77 IEGHKMTVvevdGVYVNpftvDSLDIFP--GQrySVLVTANQdPGNyWIVASPNIPA 131
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 87-192 7.46e-03

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: 38.43  E-value: 7.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88758619   87 GPTLYAEVGDIIKVHFKNKADKPLSIHPQGI--RYSKLSEGASYLDHTfpaekmddAVAPGREYTYEWSISEDSGpthdd 164
Cdd:cd13850   28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGIlqRGTPWSDGVPGVTQW--------PIQPGGSFTYRWKAEDQYG----- 94

                         90       100
                 ....*....|....*....|....*...
gi 88758619  165 ppclTHIYYSHENliEDFNSGLIGPLLI 192
Cdd:cd13850   95 ----LYWYHSHYR--GYYMDGLYGPIYI 116
 
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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