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Conserved domains on  [gi|1131184096|ref|XP_019832075|]
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PREDICTED: LOW QUALITY PROTEIN: coagulation factor V [Bos indicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1483-1654 1.02e-115

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: 363.39  E-value: 1.02e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1483 RKYYYIAAEEISWDYSKFVQSDDI-DYVPEDTVYKKVVFRKYLDSTFTKLDPQGEYEEHLGILGPVIRAEVDDVIQVRFK 1561
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGYGKSRLDkTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQVFFK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1562 NLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSAVNPEKDIH 1641
Cdd:cd14451     81 NLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKDIH 160

                          170
                   ....*....|...
gi 1131184096 1642 SGLIGPLLICRKG 1654
Cdd:cd14451    161 SGLIGPLLICRKG 173
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 32-196 3.20e-106

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: 336.06  E-value: 3.20e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   32 RQFYVAAQSIRWNYRPESTHLSSKPFETSFKKIVYREYEAYFQKEKPQSRTSGLLGPTLYAEVGDIMKVHFKNKAHKPLS 111
Cdd:cd04226      1 REYYIAAQNIDWDYTPQSEELRLKRSEQSFKKIVYREYEEGFKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  112 IHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEDSGPTHDDPPCLTHIYYSYVNLVEDFNSGLIGPLL 191
Cdd:cd04226     81 IHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALL 160


                   ....*
gi 1131184096  192 ICKKG 196
Cdd:cd04226    161 ICKKG 165
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 348-527 7.65e-105

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: 332.61  E-value: 7.65e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  348 KRWEYFIAAEEVIWDYAPIIPANMDKKYRSLHLDNFSNRIGKHYKKVVYKQYQDDSFTKRLEDPSSEGDGILGPIIRAQV 427
Cdd:cd14450      1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILGPVIRAQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  428 RDTLKIVFKNMASRSYSIYPHGVTFSPYDNEVNSSSASGSN-TMIRAVRPGETYTYKWNILESDEPTENDAQCLTRPYYS 506
Cdd:cd14450     81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNeTQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHS 160

                          170       180
                   ....*....|....*....|.
gi 1131184096  507 NVDITRDLASGLIGLLLICKS 527
Cdd:cd14450    161 AVDITRDIASGLIGPLLICKS 181
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1666-1802 1.42e-85

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: 275.98  E-value: 1.42e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1666 MREFVLLFMVFDEKKSWYYDKKPTRSWRR---ASSEVKNSHEFHAINGMIYNLPGLRMYEQEWVRLHLLNLGGSRDIHVV 1742
Cdd:cd14455      1 RREFVLLFMTFDEEKSWYYEKNRKRTCREnrvKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1743 HFHGQTLLENGTQQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLI 1802
Cdd:cd14455     81 HFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 540-683 2.55e-85

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: 275.21  E-value: 2.55e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  540 DIEQQAVFAVFDENKSWYIEDNIYKFCENPEKVKRDDPKFYESNIMSTINGYVPESIPILGFCFDDTVQWHFCSVGTQND 619
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131184096  620 IFTIHFTGHSFIYGKRHEDTLTLFPMQGESVTVTMDNVGTWMLTTMNSNPRSKKLRLRFRDAKC 683
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 208-326 5.64e-75

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: 244.77  E-value: 5.64e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  208 EKQHVLMFAVFDESKSWNQT----SSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPELFTIHFNGQVLEQNHHKI 283
Cdd:cd14453      1 YKEYVLMFGVFDENKSWYKQnasvDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNGQVLEQNGHKV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1131184096  284 SAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDI 326
Cdd:cd14453     81 SAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1968-2120 6.67e-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: 191.03  E-value: 6.67e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1968 TPLGMESGKiENKQITASSfkksWWGNYWEPFLARLNAqghVNAWQAKANNNNQWLQIDLLKIKKITAIVTQGCKSLSSE 2047
Cdd:cd00057      1 EPLGMESGL-ADDQITASS----SYSSGWEASRARLNS---DNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131184096 2048 MYVKSYTIHYSDQGTDWKPYREKssMVDKIFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWNQSIALRLELFG 2120
Cdd:cd00057     73 EWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1809-1960 2.46e-50

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: 175.23  E-value: 2.46e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1809 MPMGLSTGLiADSQIQASEFWGY-WEPKLARLNnggSYNAWIAEKLstefNPEPWIQVDMQKEVLLTGIQTQGAKHYLKP 1887
Cdd:cd00057      1 EPLGMESGL-ADDQITASSSYSSgWEASRARLN---SDNAWTPAVN----DPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131184096 1888 YYTTEFCVAYSLDRKNWR*FKGNStrNVMYFGGNSDASTIKENQIDPPVVARYIRISPTGSYNKPALRLELQG 1960
Cdd:cd00057     73 EWVTSYKVQYSLDGETWTTYKDKG--EEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1083-1400 1.38e-07

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 56.85  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1083 DQTSPNDTTSqTSSPPDLYPT---VSPEEHYQIFPIQDSDPTHSTTAPSNRSPDPTHSTTAPS-NRSPP----TQPSQIP 1154
Cdd:pfam05109  505 DMTSPTSAVT-TPTPNATSPTpavTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTpNATIPtlgkTSPTSAV 583

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1155 NYDLRNRAIPTdVSQIFPSlelevwQTATSLDLSQPSISPdlgqMALSPdPGQESLSPDLGQTSL-SPDLSQESLSPDLG 1233
Cdd:pfam05109  584 TTPTPNATSPT-VGETSPQ------ANTTNHTLGGTSSTP----VVTSP-PKNATSAVTTGQHNItSSSTSSMSLRPSSI 651

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1234 QTALSPDPSQESLSPDLGQTSLSPDlGQESLSPDLGQTALSPDPSQESLSPDLGQTSLSPDLGQTALSPDPSQESL---S 1310
Cdd:pfam05109  652 SETLSPSTSDNSTSHMPLLTSAHPT-GGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVtkgT 730

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1311 PDLGQTSLSPDLGQESLSPDLGQTALSPDLSL----------ESLSPDLSQLDLKQTSPPLDLNQTSHTSESSQSLPLPE 1380
Cdd:pfam05109  731 PPKNATSPQAPSGQKTAVPTVTSTGGKANSTTggkhttghgaRTSTEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPR 810

                          330       340
                   ....*....|....*....|.
gi 1131184096 1381 FGQTFPNADIGQMPSP-PPDS 1400
Cdd:pfam05109  811 WTFTSPPVTTAQATVPvPPTS 831
 
Name Accession Description Interval E-value
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1483-1654 1.02e-115

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: 363.39  E-value: 1.02e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1483 RKYYYIAAEEISWDYSKFVQSDDI-DYVPEDTVYKKVVFRKYLDSTFTKLDPQGEYEEHLGILGPVIRAEVDDVIQVRFK 1561
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGYGKSRLDkTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQVFFK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1562 NLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSAVNPEKDIH 1641
Cdd:cd14451     81 NLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKDIH 160

                          170
                   ....*....|...
gi 1131184096 1642 SGLIGPLLICRKG 1654
Cdd:cd14451    161 SGLIGPLLICRKG 173
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 32-196 3.20e-106

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: 336.06  E-value: 3.20e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   32 RQFYVAAQSIRWNYRPESTHLSSKPFETSFKKIVYREYEAYFQKEKPQSRTSGLLGPTLYAEVGDIMKVHFKNKAHKPLS 111
Cdd:cd04226      1 REYYIAAQNIDWDYTPQSEELRLKRSEQSFKKIVYREYEEGFKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  112 IHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEDSGPTHDDPPCLTHIYYSYVNLVEDFNSGLIGPLL 191
Cdd:cd04226     81 IHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALL 160


                   ....*
gi 1131184096  192 ICKKG 196
Cdd:cd04226    161 ICKKG 165
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 348-527 7.65e-105

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: 332.61  E-value: 7.65e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  348 KRWEYFIAAEEVIWDYAPIIPANMDKKYRSLHLDNFSNRIGKHYKKVVYKQYQDDSFTKRLEDPSSEGDGILGPIIRAQV 427
Cdd:cd14450      1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILGPVIRAQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  428 RDTLKIVFKNMASRSYSIYPHGVTFSPYDNEVNSSSASGSN-TMIRAVRPGETYTYKWNILESDEPTENDAQCLTRPYYS 506
Cdd:cd14450     81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNeTQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHS 160

                          170       180
                   ....*....|....*....|.
gi 1131184096  507 NVDITRDLASGLIGLLLICKS 527
Cdd:cd14450    161 AVDITRDIASGLIGPLLICKS 181
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1666-1802 1.42e-85

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: 275.98  E-value: 1.42e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1666 MREFVLLFMVFDEKKSWYYDKKPTRSWRR---ASSEVKNSHEFHAINGMIYNLPGLRMYEQEWVRLHLLNLGGSRDIHVV 1742
Cdd:cd14455      1 RREFVLLFMTFDEEKSWYYEKNRKRTCREnrvKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1743 HFHGQTLLENGTQQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLI 1802
Cdd:cd14455     81 HFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 540-683 2.55e-85

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: 275.21  E-value: 2.55e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  540 DIEQQAVFAVFDENKSWYIEDNIYKFCENPEKVKRDDPKFYESNIMSTINGYVPESIPILGFCFDDTVQWHFCSVGTQND 619
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131184096  620 IFTIHFTGHSFIYGKRHEDTLTLFPMQGESVTVTMDNVGTWMLTTMNSNPRSKKLRLRFRDAKC 683
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 208-326 5.64e-75

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: 244.77  E-value: 5.64e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  208 EKQHVLMFAVFDESKSWNQT----SSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPELFTIHFNGQVLEQNHHKI 283
Cdd:cd14453      1 YKEYVLMFGVFDENKSWYKQnasvDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNGQVLEQNGHKV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1131184096  284 SAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDI 326
Cdd:cd14453     81 SAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1968-2120 6.67e-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: 191.03  E-value: 6.67e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1968 TPLGMESGKiENKQITASSfkksWWGNYWEPFLARLNAqghVNAWQAKANNNNQWLQIDLLKIKKITAIVTQGCKSLSSE 2047
Cdd:cd00057      1 EPLGMESGL-ADDQITASS----SYSSGWEASRARLNS---DNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131184096 2048 MYVKSYTIHYSDQGTDWKPYREKssMVDKIFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWNQSIALRLELFG 2120
Cdd:cd00057     73 EWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1809-1960 2.46e-50

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: 175.23  E-value: 2.46e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1809 MPMGLSTGLiADSQIQASEFWGY-WEPKLARLNnggSYNAWIAEKLstefNPEPWIQVDMQKEVLLTGIQTQGAKHYLKP 1887
Cdd:cd00057      1 EPLGMESGL-ADDQITASSSYSSgWEASRARLN---SDNAWTPAVN----DPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131184096 1888 YYTTEFCVAYSLDRKNWR*FKGNStrNVMYFGGNSDASTIKENQIDPPVVARYIRISPTGSYNKPALRLELQG 1960
Cdd:cd00057     73 EWVTSYKVQYSLDGETWTTYKDKG--EEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1806-1961 1.77e-38

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


Pssm-ID: 214572  Cd Length: 139  Bit Score: 141.11  E-value: 1.77e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  1806 ECKMPMGLSTgliaDSQIQASEfwGYWEPKLARLNnGGSYNAWIAEKLStefnPEPWIQVDMQKEVLLTGIQTQGAKHyl 1885
Cdd:smart00231    1 PCNEPLGLES----DSQITASS--SYWAAKIARLN-GGSDGGWCPAKND----LPPWIQVDLGRLRTVTGVITGRRHG-- 67

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131184096  1886 KPYYTTEFCVaYSLDRKNWR*FKGnstRNVMYFGGNSDASTIKENQIDPPVVARYIRISPTGSYNKPALRLELQGC 1961
Cdd:smart00231   68 NGDWVTYKLE-YSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1965-2121 1.25e-35

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: 133.02  E-value: 1.25e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  1965 GCSTPLGMESgkieNKQITASSfkkswwgNYWEPFLARLNaQGHVNAWQAKANNNNQWLQIDLLKIKKITAIVTQGCKSL 2044
Cdd:smart00231    1 PCNEPLGLES----DSQITASS-------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHGN 68

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131184096  2045 SSEMYvksYTIHYSDQGTDWKPYREKSSMVdkiFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWNQSIALRLELFGC 2121
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.
 1981-2118 1.63e-32

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: 123.33  E-value: 1.63e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1981 QITASSfkkSWWGNYwePFLARLNaqGHVN-AWQAKANNNNQWLQIDLLKIKKITAIVTQGCKSLSSeMYVKSYTIHYSD 2059
Cdd:pfam00754    1 QITASS---SYSGEG--PAAAALD--GDPNtAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSN-GYVTSYKIEYSL 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131184096 2060 QGTDWKPYRekssmvDKIFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWN--QSIALRLEL 2118
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.
 1822-1958 8.53e-26

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


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 104.45  E-value: 8.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1822 QIQASEFWGYWEPKLARLNNGGSyNAWIaeklSTEFNPEPWIQVDMQKEVLLTGIQTQGAKHyLKPYYTTEFCVAYSLDR 1901
Cdd:pfam00754    1 QITASSSYSGEGPAAAALDGDPN-TAWS----AWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131184096 1902 KNWR*FKGNSTRnvmyfgGNSDASTIKENQIDPPVVARYIRISPTG--SYNKPALRLEL 1958
Cdd:pfam00754   75 ENWTTVKDEKIP------GNNDNNTPVTNTFDPPIKARYVRIVPTSwnGGNGIALRAEL 127
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1543-1737 1.06e-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: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1543 ILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGL--SYEkssegktyEDDSPEwfkedNAIQPNKTYTYVWHATTRSG--- 1617
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLrvPNA--------MDGVPG-----DPIAPGETFTYEFPVPQPAGtyw 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1618 --PENPGSacrawayySAVNpekdIHSGLIGPLLIcrkgtLDKETNMPVDMREFVLLF--MVFDEKKSWYYDkkptrswr 1693
Cdd:COG2132    109 yhPHTHGS--------TAEQ----VYRGLAGALIV-----EDPEEDLPRYDRDIPLVLqdWRLDDDGQLLYP-------- 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1131184096 1694 RASSEVKNSHEFHAINGMIynLPGLRMYEQEWVRLHLLNLGGSR 1737
Cdd:COG2132    164 MDAAMGGRLGDTLLVNGRP--NPTLEVRPGERVRLRLLNASNAR 205
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1083-1400 1.38e-07

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 56.85  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1083 DQTSPNDTTSqTSSPPDLYPT---VSPEEHYQIFPIQDSDPTHSTTAPSNRSPDPTHSTTAPS-NRSPP----TQPSQIP 1154
Cdd:pfam05109  505 DMTSPTSAVT-TPTPNATSPTpavTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTpNATIPtlgkTSPTSAV 583

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1155 NYDLRNRAIPTdVSQIFPSlelevwQTATSLDLSQPSISPdlgqMALSPdPGQESLSPDLGQTSL-SPDLSQESLSPDLG 1233
Cdd:pfam05109  584 TTPTPNATSPT-VGETSPQ------ANTTNHTLGGTSSTP----VVTSP-PKNATSAVTTGQHNItSSSTSSMSLRPSSI 651

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1234 QTALSPDPSQESLSPDLGQTSLSPDlGQESLSPDLGQTALSPDPSQESLSPDLGQTSLSPDLGQTALSPDPSQESL---S 1310
Cdd:pfam05109  652 SETLSPSTSDNSTSHMPLLTSAHPT-GGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVtkgT 730

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1311 PDLGQTSLSPDLGQESLSPDLGQTALSPDLSL----------ESLSPDLSQLDLKQTSPPLDLNQTSHTSESSQSLPLPE 1380
Cdd:pfam05109  731 PPKNATSPQAPSGQKTAVPTVTSTGGKANSTTggkhttghgaRTSTEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPR 810

                          330       340
                   ....*....|....*....|.
gi 1131184096 1381 FGQTFPNADIGQMPSP-PPDS 1400
Cdd:pfam05109  811 WTFTSPPVTTAQATVPvPPTS 831
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 85-192 1.03e-06

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: 49.55  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   85 LLGPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIKYSK--FSEGASYSDHtlpmekmdDAVAPGQEYTYEWIISEDSGpth 162
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGtpWMDGVPGVTQ--------CPIPPGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 1131184096  163 ddppclTHIYYSYVNLVEdfNSGLIGPLLI 192
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 85-247 3.68e-06

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: 51.86  E-value: 3.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   85 LLGPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIkyskfsegasysdhTLPMEkMD----DAVAPGQEYTYEWIIsedsgp 160
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL--------------RVPNA-MDgvpgDPIAPGETFTYEFPV------ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  161 thDDPPClTHIYYSYVNLVEDFN--SGLIGPLLIckkgtltEDGTQKM--FEKQHVLMFAvfDesKSWNQTSSLMYTVNG 236
Cdd:COG2132    101 --PQPAG-TYWYHPHTHGSTAEQvyRGLAGALIV-------EDPEEDLprYDRDIPLVLQ--D--WRLDDDGQLLYPMDA 166

                          170
                   ....*....|..
gi 1131184096  237 YVNGTMPD-ITV 247
Cdd:COG2132    167 AMGGRLGDtLLV 178
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1051-1398 6.81e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.71  E-value: 6.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1051 LLHASNETSLSIDLNQTFPSMNLSLAASLPDHDQTSPndTTSQTSSPPDLYPTVSPEEHYQIFPIQDSDPTHSTTAPSNR 1130
Cdd:PHA03307    35 LLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGP--PPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPS 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1131 SPDPTHSTTAPSNRSPPTQPSQIPNYDLRNRAIPTDV-SQIFPSLELEVWQ--TATSLDLSQPSISPDlgQMALSPDPGQ 1207
Cdd:PHA03307   113 SPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAaSPPAAGASPAAVAsdAASSRQAALPLSSPE--ETARAPSSPP 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1208 ESLSPDLGQTSLSPDLSqeSLSPDLGQTALSPDPSQESLSPDLGQTSLSPDLGQESLSPDLGQTALSPDPsqeslSPDLG 1287
Cdd:PHA03307   191 AEPPPSTPPAAASPRPP--RRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLP-----RPAPI 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1288 QTSLSPDLGQTALSPDPSQESLSPDLGQTSLSPDlgQESLSPDLGQTALSPDLSLESLSPDLSQLDLKQTSPPLDLNQTS 1367
Cdd:PHA03307   264 TLPTRIWEASGWNGPSSRPGPASSSSSPRERSPS--PSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAV 341

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1131184096 1368 HTSESSQSLPLPefGQTFPNADigqmPSPPP 1398
Cdd:PHA03307   342 SPGPSPSRSPSP--SRPPPPAD----PSSPR 366
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1543-1617 1.09e-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: 40.69  E-value: 1.09e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131184096 1543 ILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSegktYEDDSPEWfkEDNAIQPNKTYTYVWHATTRSG 1617
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTP----WMDGVPGV--TQCPIPPGQSFTYRFQVKQQAG 92
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 587-669 1.70e-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: 40.76  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  587 TINGYVPESIPILGFCFDDTVQWHFCSVGTqNDIFTIHFTGHSFIY----GKRHE----DTLTLFPMQGESVTVTMDN-V 657
Cdd:pfam00394   40 LINGKDGASLATLTVTPGKTYRLRIINVAL-DDSLNFSIEGHKMTVvevdGVYVNpftvDSLDIFPGQRYSVLVTANQdP 118

                           90
                   ....*....|..
gi 1131184096  658 GTWMLTTMNSNP 669
Cdd:pfam00394  119 GNYWIVASPNIP 130
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1705-1806 2.11e-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: 40.50  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1705 FHAINGMIY--NLPGLRMYEQEWVRLHLLNLGGsrDIHVVHFHGQT--LLENGTQQHQL----------GVW----PLLP 1766
Cdd:pfam07731   21 DWAINGLLFppNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSfqVLGRGGGPWPEedpktynlvdPVRrdtvQVPP 98

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1131184096 1767 GSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLIVDRE 1806
Cdd:pfam07731   99 GGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 418-486 6.27e-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: 38.77  E-value: 6.27e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131184096  418 ILGPIIRAQVRDTLKIVFKNMASRSYSIYPHG--VTFSPYDNEVNsssaSGSNTMIravRPGETYTYKWNI 486
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGlqQRGTPWMDGVP----GVTQCPI---PPGQSFTYRFQV 87
 
Name Accession Description Interval E-value
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1483-1654 1.02e-115

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: 363.39  E-value: 1.02e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1483 RKYYYIAAEEISWDYSKFVQSDDI-DYVPEDTVYKKVVFRKYLDSTFTKLDPQGEYEEHLGILGPVIRAEVDDVIQVRFK 1561
Cdd:cd14451      1 KRRYYIAAEEEEWDYAGYGKSRLDkTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGPVIRAEVDDVIQVFFK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1562 NLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSAVNPEKDIH 1641
Cdd:cd14451     81 NLASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKDIH 160

                          170
                   ....*....|...
gi 1131184096 1642 SGLIGPLLICRKG 1654
Cdd:cd14451    161 SGLIGPLLICRKG 173
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 32-196 3.20e-106

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: 336.06  E-value: 3.20e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   32 RQFYVAAQSIRWNYRPESTHLSSKPFETSFKKIVYREYEAYFQKEKPQSRTSGLLGPTLYAEVGDIMKVHFKNKAHKPLS 111
Cdd:cd04226      1 REYYIAAQNIDWDYTPQSEELRLKRSEQSFKKIVYREYEEGFKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  112 IHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEDSGPTHDDPPCLTHIYYSYVNLVEDFNSGLIGPLL 191
Cdd:cd04226     81 IHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALL 160


                   ....*
gi 1131184096  192 ICKKG 196
Cdd:cd04226    161 ICKKG 165
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 348-527 7.65e-105

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: 332.61  E-value: 7.65e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  348 KRWEYFIAAEEVIWDYAPIIPANMDKKYRSLHLDNFSNRIGKHYKKVVYKQYQDDSFTKRLEDPSSEGDGILGPIIRAQV 427
Cdd:cd14450      1 KNWEYFIAAEEVIWDYAPSIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILGPVIRAQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  428 RDTLKIVFKNMASRSYSIYPHGVTFSPYDNEVNSSSASGSN-TMIRAVRPGETYTYKWNILESDEPTENDAQCLTRPYYS 506
Cdd:cd14450     81 RDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNeTQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHS 160

                          170       180
                   ....*....|....*....|.
gi 1131184096  507 NVDITRDLASGLIGLLLICKS 527
Cdd:cd14450    161 AVDITRDIASGLIGPLLICKS 181
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 1484-1653 8.92e-88

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: 283.53  E-value: 8.92e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1484 KYYYIAAEEISWDYSKFVQSD----------DIDYVPEDTVYKKVVFRKYLDSTFTKLdpqGEYEEHLGILGPVIRAEVD 1553
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEkdlsyrnqylDNGPFRIGRSYKKVVYREYTDESFTTP---GPQPEHLGILGPTIRAEVG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1554 DVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSA 1633
Cdd:cd04199     78 DTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSH 157

                          170       180
                   ....*....|....*....|
gi 1131184096 1634 VNPEKDIHSGLIGPLLICRK 1653
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 ...
 1666-1802 1.42e-85

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: 275.98  E-value: 1.42e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1666 MREFVLLFMVFDEKKSWYYDKKPTRSWRR---ASSEVKNSHEFHAINGMIYNLPGLRMYEQEWVRLHLLNLGGSRDIHVV 1742
Cdd:cd14455      1 RREFVLLFMTFDEEKSWYYEKNRKRTCREnrvKDPNVQDNHTFHAINGIIYNLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1743 HFHGQTLLENGTQQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLI 1802
Cdd:cd14455     81 HFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 540-683 2.55e-85

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: 275.21  E-value: 2.55e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  540 DIEQQAVFAVFDENKSWYIEDNIYKFCENPEKVKRDDPKFYESNIMSTINGYVPESIPILGFCFDDTVQWHFCSVGTQND 619
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131184096  620 IFTIHFTGHSFIYGKRHEDTLTLFPMQGESVTVTMDNVGTWMLTTMNSNPRSKKLRLRFRDAKC 683
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 ...
 32-195 6.76e-85

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: 275.44  E-value: 6.76e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   32 RQFYVAAQSIRWNYRPESTH------------LSSKPFETSFKKIVYREYEAYFQKE-KPQSRTSGLLGPTLYAEVGDIM 98
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAekdlsyrnqyldNGPFRIGRSYKKVVYREYTDESFTTpGPQPEHLGILGPTIRAEVGDTI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   99 KVHFKNKAHKPLSIHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEDSGPTHDDPPCLTHIYYSYVNL 178
Cdd:cd04199     81 KVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHVDL 160

                          170
                   ....*....|....*..
gi 1131184096  179 VEDFNSGLIGPLLICKK 195
Cdd:cd04199    161 EKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 350-527 7.03e-84

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: 272.36  E-value: 7.03e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  350 WEYFIAAEEVIWDYAPIIPANMDKKYRSLHLDNFSNRIGKHYKKVVYKQYQDDSFTKRLEDPssEGDGILGPIIRAQVRD 429
Cdd:cd04199      1 RHYYIAAEEIDWDYAPSGLAEKDLSYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQP--EHLGILGPTIRAEVGD 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  430 TLKIVFKNMASRSYSIYPHGVTFSPYDNEVNSSSASGS-NTMIRAVRPGETYTYKWNILESDEPTENDAQCLTRPYYSNV 508
Cdd:cd04199     79 TIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPdEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHV 158

                          170
                   ....*....|....*....
gi 1131184096  509 DITRDLASGLIGLLLICKS 527
Cdd:cd04199    159 DLEKDINSGLIGPLLICKK 177
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 208-326 5.64e-75

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: 244.77  E-value: 5.64e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  208 EKQHVLMFAVFDESKSWNQT----SSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPELFTIHFNGQVLEQNHHKI 283
Cdd:cd14453      1 YKEYVLMFGVFDENKSWYKQnasvDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNGQVLEQNGHKV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1131184096  284 SAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDI 326
Cdd:cd14453     81 SAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 540-680 1.74e-65

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: 218.43  E-value: 1.74e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  540 DIEQQAVFAVFDENKSWYIEDNIYKFCENPEKVKRDDPKFYESNIMSTINGYVPESIPILGFCFDDTVQWHFCSVGTQND 619
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131184096  620 IFTIHFTGHSFIYGKRHEDTLTLFPMQGESVTVTMDNVGTWMLTTMNSNPRSKKLRLRFRD 680
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1481-1657 4.62e-60

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: 205.01  E-value: 4.62e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1481 GNRKYYYIAAEEISWDYS----------KFVQSDDIDYV---PEDT----VYKKVVFRKYLDSTFTKLDPQGEYEEHLGI 1543
Cdd:cd04224      1 GKVRHYFIAAEEIMWDYApsgknlftgqNLTAPGSDSEVffqRNETriggTYWKVRYVEYTDATFTTRKHRSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1544 LGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPewfKEDNAIQPNKTYTYVWHATTRSGPENPGS 1623
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDP---SPGSHVSPGETFTYEWTVPEGVGPTNQDP 157

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1131184096 1624 ACRAWAYYSAVNPEKDIHSGLIGPLLICRKGTLD 1657
Cdd:cd04224    158 PCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLN 191
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 1666-1802 1.35e-58

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: 198.79  E-value: 1.35e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1666 MREFVLLFMVFDEKKSWYYDKKPTRSWR------RASSEVKNSHEFHAINGMIY-NLPGLRMYEQEWVRLHLLNLGGSRD 1738
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEDNIKRFCDnpekvdKDDEEFQESNKMHAINGYVFgNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131184096 1739 IHVVHFHGQTLLENGtqqHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLI 1802
Cdd:cd04200     81 VHSIHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 348-526 1.98e-58

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: 199.77  E-value: 1.98e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  348 KRWEYFIAAEEVIWDYAPIIPANMDKKYRSLHLDNFSNRIGKHYKKVVYKQYQDDSFTKRleDPSSEGDGILGPIIRAQV 427
Cdd:cd04227      1 QTWEHYIAAEELDWDYAPLLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRR--EAKQTEKGILGPLLKGEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  428 RDTLKIVFKNMASRSYSIYPHGVT-FSPYDNEVNSSSASGSNTMirAVRPGETYTYKWNILESDEPTENDAQCLTRPYYS 506
Cdd:cd04227     79 GDQIHIMFKNTASRPYNIYPHGLTsVRPMYRSRNPAGEKDLKTM--PIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQS 156

                          170       180
                   ....*....|....*....|
gi 1131184096  507 NVDITRDLASGLIGLLLICK 526
Cdd:cd04227    157 TVDPERDLASGLIGPLLICK 176
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 30-205 2.48e-58

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: 200.39  E-value: 2.48e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   30 KLRQFYVAAQSIRWNYRPESTHLS-----------SKPFET--------SFKKIVYREY-EAYFQKEKPQSRTS---GLL 86
Cdd:cd04224      2 KVRHYFIAAEEIMWDYAPSGKNLFtgqnltapgsdSEVFFQrnetriggTYWKVRYVEYtDATFTTRKHRSKEEehlGIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   87 GPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIKYSKFSEGASYSDHTLPMEKMddaVAPGQEYTYEWIISEDSGPTHDDPP 166
Cdd:cd04224     82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSH---VSPGETFTYEWTVPEGVGPTNQDPP 158

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1131184096  167 CLTHIYYSYVNLVEDFNSGLIGPLLICKKGTLTEDGTQK 205
Cdd:cd04224    159 CLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1968-2120 6.67e-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: 191.03  E-value: 6.67e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1968 TPLGMESGKiENKQITASSfkksWWGNYWEPFLARLNAqghVNAWQAKANNNNQWLQIDLLKIKKITAIVTQGCKSLSSE 2047
Cdd:cd00057      1 EPLGMESGL-ADDQITASS----SYSSGWEASRARLNS---DNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131184096 2048 MYVKSYTIHYSDQGTDWKPYREKssMVDKIFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWNQSIALRLELFG 2120
Cdd:cd00057     73 EWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 352-537 2.36e-55

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: 191.53  E-value: 2.36e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  352 YFIAAEEVIWDYAPiipanMDKKYRS------------LHLDNFSNRIGKHYKKVVYKQYQDDSFTKRLE-DPSSEGDGI 418
Cdd:cd04224      6 YFIAAEEIMWDYAP-----SGKNLFTgqnltapgsdseVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHrSKEEEHLGI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  419 LGPIIRAQVRDTLKIVFKNMASRSYSIYPHGVTF------SPYDNEVNSSSASgsntmiraVRPGETYTYKWNILESDEP 492
Cdd:cd04224     81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYeknyegAMYRDGDPSPGSH--------VSPGETFTYEWTVPEGVGP 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1131184096  493 TENDAQCLTRPYYSNVDITRDLASGLIGLLLICKSRSLDRRGIQR 537
Cdd:cd04224    153 TNQDPPCLTYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1484-1654 7.05e-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: 183.55  E-value: 7.05e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1484 KYYYIAAEEISWDYS-----KFVQSDDID-----YVPEdtvYKKVVFRKYLDSTFTKLDPQGEYEEHLGILGPVIRAEVD 1553
Cdd:cd04228      2 RHYFIAAVEVLWDYGmqrpqHFLRARDPNrgrrkSVPQ---YKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIRAEVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1554 DVIQVRFKNLASRPYSLHAHGLSYEkssegktyEDDSPEWFKedNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSA 1633
Cdd:cd04228     79 DNIMVTFKNLASRPYSFHSSLISYE--------EDQRAEPRG--NFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSN 148

                          170       180
                   ....*....|....*....|.
gi 1131184096 1634 VNPEKDIHSGLIGPLLICRKG 1654
Cdd:cd04228    149 VDLEKDLHSGLIGPLIICKTG 169
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1486-1654 2.01e-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: 2.01e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1486 YYIAAEEISWDYskfVQSDDIDYV------PEDT--VYKKVVFRKYLDSTFTKLDPQGEYeehLGILGPVIRAEVDDVIQ 1557
Cdd:cd14452      3 YYIAAVEIGWDY---IHSDLGDPAseqrkkPKDIpqKYIKAVFVEYLDATFTVPKPRPAW---MGLLGPTIVAEVGDTVV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1558 VRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSAVNPE 1637
Cdd:cd14452     77 ITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPV 156

                          170
                   ....*....|....*..
gi 1131184096 1638 KDIHSGLIGPLLICRKG 1654
Cdd:cd14452    157 KDVNSGLIGALLVCRMG 173
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1484-1653 4.06e-51

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: 178.43  E-value: 4.06e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1484 KYYYIAAEEISWDYS-------------------KFVQSDDiDYVpeDTVYKKVVFRKYLDSTFTKLDPQGEYEEHLGIL 1544
Cdd:cd04225      1 RTYYIAAEEVEWDYSpqrtweqelhntheespgnAFLNKGD-KFI--GSKYKKVVYREYTDDTFSVPKERTAEEEHLGIL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1545 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTyeddspewfkednaiQPNKTYTYVWHATTRSGPENPGSA 1624
Cdd:cd04225     78 GPLIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPT---------------EPGETQTYTWKIPERSGPGVEDSN 142

                          170       180
                   ....*....|....*....|....*....
gi 1131184096 1625 CRAWAYYSAVNPEKDIHSGLIGPLLICRK 1653
Cdd:cd04225    143 CISWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 351-526 8.68e-51

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: 178.00  E-value: 8.68e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  351 EYFIAAEEVIWDYAP----IIPANM--DKKYRSLHLDNFSNRIGKHYKKVVYKQYQDDSFTKRLEDPSSEGdgILGPIIR 424
Cdd:cd04222      2 EYYIGIRETQWDYAPsgknLITNQTfdDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLG--FLGPILK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  425 AQVRDTLKIVFKNMASRSYSIYPHGVTFSPyDNE--VNSSSASGSNTMIRAVRPGETYTYKWNILESDEPTENDAQCLTR 502
Cdd:cd04222     80 AEVGDVIVVHLKNFASRPYSLHPHGVFYNK-ENEgaLYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTR 158

                          170       180
                   ....*....|....*....|....
gi 1131184096  503 PYYSNVDITRDLASGLIGLLLICK 526
Cdd:cd04222    159 IYHSHIDAPKDIASGLIGPLIICK 182
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 32-196 8.73e-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: 177.48  E-value: 8.73e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   32 RQFYVAAQSIRWNYR-----PESTHLSSKPFETS--FKKIVYREY-EAYFQKEKPQSRTSGLLGPTLYAEVGDIMKVHFK 103
Cdd:cd14452      1 RRYYIAAVEIGWDYIhsdlgDPASEQRKKPKDIPqkYIKAVFVEYlDATFTVPKPRPAWMGLLGPTIVAEVGDTVVITFK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  104 NKAHKPLSIHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEDSGPTHDDPPCLTHIYYSYVNLVEDFN 183
Cdd:cd14452     81 NLASQPYSLHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVKDVN 160

                          170
                   ....*....|...
gi 1131184096  184 SGLIGPLLICKKG 196
Cdd:cd14452    161 SGLIGALLVCRMG 173
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 208-326 9.35e-51

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: 176.06  E-value: 9.35e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  208 EKQHVLMFAVFDESKSWNQT----------------------SSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPE 265
Cdd:cd04200      1 DKEFVLLFAVFDENKSWYLEdnikrfcdnpekvdkddeefqeSNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131184096  266 LFTIHFNGQVLEQNHHKISAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDI 326
Cdd:cd04200     81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1809-1960 2.46e-50

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: 175.23  E-value: 2.46e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1809 MPMGLSTGLiADSQIQASEFWGY-WEPKLARLNnggSYNAWIAEKLstefNPEPWIQVDMQKEVLLTGIQTQGAKHYLKP 1887
Cdd:cd00057      1 EPLGMESGL-ADDQITASSSYSSgWEASRARLN---SDNAWTPAVN----DPPQWLQVDLGKTRRVTGIQTQGRKGGGSS 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131184096 1888 YYTTEFCVAYSLDRKNWR*FKGNStrNVMYFGGNSDASTIKENQIDPPVVARYIRISPTGSYNKPALRLELQG 1960
Cdd:cd00057     73 EWVTSYKVQYSLDGETWTTYKDKG--EEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1484-1653 3.85e-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: 176.07  E-value: 3.85e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1484 KYYYIAAEEISWDYS---------KFVQSDDIDYV-----PE--DTVYKKVVFRKYLDSTFTKLDPQGEYeehLGILGPV 1547
Cdd:cd04222      1 REYYIGIRETQWDYApsgknlitnQTFDDDEHASVflkrgPDriGRVYKKAVYLQYTDDTYRTEIEKPVW---LGFLGPI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1548 IRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRA 1627
Cdd:cd04222     78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                          170       180
                   ....*....|....*....|....*.
gi 1131184096 1628 WAYYSAVNPEKDIHSGLIGPLLICRK 1653
Cdd:cd04222    158 RIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 32-195 3.96e-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: 176.07  E-value: 3.96e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   32 RQFYVAAQSIRWNYRPESTHL-SSKPFETS-----------------FKKIVYREY-EAYFQKEKPQSRTSGLLGPTLYA 92
Cdd:cd04222      1 REYYIGIRETQWDYAPSGKNLiTNQTFDDDehasvflkrgpdrigrvYKKAVYLQYtDDTYRTEIEKPVWLGFLGPILKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   93 EVGDIMKVHFKNKAHKPLSIHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEDSGPTHDDPPCLTHIY 172
Cdd:cd04222     81 EVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                          170       180
                   ....*....|....*....|...
gi 1131184096  173 YSYVNLVEDFNSGLIGPLLICKK 195
Cdd:cd04222    161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 1484-1654 5.12e-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: 175.05  E-value: 5.12e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1484 KYYYIAAEEISWDYSKfvQSDDIDYVPEDTVYKKVVFRKYlDSTFTKLDPQGEYEehlGILGPVIRAEVDDVIQVRFKNL 1563
Cdd:cd04226      1 REYYIAAQNIDWDYTP--QSEELRLKRSEQSFKKIVYREY-EEGFKKEKPADLSS---GLLGPTLRAEVGDTLIVHFKNM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1564 ASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSAVNPEKDIHSG 1643
Cdd:cd04226     75 ADKPLSIHPQGIAYGKKSEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSG 154

                          170
                   ....*....|.
gi 1131184096 1644 LIGPLLICRKG 1654
Cdd:cd04226    155 LIGALLICKKG 165
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 352-526 1.07e-49

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: 174.58  E-value: 1.07e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  352 YFIAAEEVIWDYAPiiPANMDKKYRSLHLDNFSN--------RIGKHYKKVVYKQYQDDSFTKRLEDPSSEGD-GILGPI 422
Cdd:cd04225      3 YYIAAEEVEWDYSP--QRTWEQELHNTHEESPGNaflnkgdkFIGSKYKKVVYREYTDDTFSVPKERTAEEEHlGILGPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  423 IRAQVRDTLKIVFKNMASRSYSIYPHGVtfspydnevnsssaSGSNTMIRAVRPGETYTYKWNILESDEPTENDAQCLTR 502
Cdd:cd04225     81 IHAEVGEKVKIVFKNMASRPYSIHAHGV--------------KTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISW 146

                          170       180
                   ....*....|....*....|....
gi 1131184096  503 PYYSNVDITRDLASGLIGLLLICK 526
Cdd:cd04225    147 AYYSTVDQIKDLYSGLIGPLVICR 170
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1486-1652 5.54e-49

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: 172.75  E-value: 5.54e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1486 YYIAAEEISWDYS-KFVQSDDIDYVPEDTV---------YKKVVFRKYLDSTFTKLDPQGEYEEhLGILGPVIRAEVDDV 1555
Cdd:cd14450      5 YFIAAEEVIWDYApSIPENMDKRYRSQYLDnfsnnigkkYKKAVFTQYEDGSFTKRLENPRPKE-EGILGPVIRAQVRDT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1556 IQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAIQPNKTYTYVWHATTRSGPENPGSACRAWAYYSAVN 1635
Cdd:cd14450     84 IKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHSAVD 163

                          170
                   ....*....|....*..
gi 1131184096 1636 PEKDIHSGLIGPLLICR 1652
Cdd:cd14450    164 ITRDIASGLIGPLLICK 180
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 32-196 4.19e-48

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: 170.02  E-value: 4.19e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   32 RQFYVAAQSIRWNYRP--ESTHLSSK-PFETSFKKIVYREY-EAYFQKEKPQSRTS---GLLGPTLYAEVGDIMKVHFKN 104
Cdd:cd14451      2 RRYYIAAEEEEWDYAGygKSRLDKTQnERDTVFKKVVFRRYlDSTFSTPDIQGEYEehlGILGPVIRAEVDDVIQVFFKN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  105 KAHKPLSIHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEDSGPTHDDPPCLTHIYYSYVNLVEDFNS 184
Cdd:cd14451     82 LASRPYSLHAHGLSYEKSSEGLSYDDESPDWFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKDIHS 161

                          170
                   ....*....|..
gi 1131184096  185 GLIGPLLICKKG 196
Cdd:cd14451    162 GLIGPLLICRKG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 33-194 9.30e-43

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: 155.03  E-value: 9.30e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   33 QFYVAAQSIRWNYRPE----------STHLSSKP--FETSFKKIVYREYE-AYFQK--EKPQSRTSGLLGPTLYAEVGDI 97
Cdd:cd14450      4 EYFIAAEEVIWDYAPSipenmdkryrSQYLDNFSnnIGKKYKKAVFTQYEdGSFTKrlENPRPKEEGILGPVIRAQVRDT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   98 MKVHFKNKAHKPLSIHAQGIKYSKFSEGASYSDHTLPMEKMDDAVAPGQEYTYEWIISEDSGPTHDDPPCLTHIYYSYVN 177
Cdd:cd14450     84 IKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHSAVD 163

                          170
                   ....*....|....*..
gi 1131184096  178 LVEDFNSGLIGPLLICK 194
Cdd:cd14450    164 ITRDIASGLIGPLLICK 180
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 351-526 2.32e-42

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: 153.50  E-value: 2.32e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  351 EYFIAAEEVIWDYApiipanMDKKYRSLHLDNFSNRIGKH---YKKVVYKQYQDDSFTkrleDPSSEGD-----GILGPI 422
Cdd:cd04228      3 HYFIAAVEVLWDYG------MQRPQHFLRARDPNRGRRKSvpqYKKVVFREYLDGSFT----QPVYRGEldehlGILGPY 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  423 IRAQVRDTLKIVFKNMASRSYSIYPHGVtfspYDNEVNSSSASGsntmiRAVRPGETYTYKWNILESDEPTENDAQCLTR 502
Cdd:cd04228     73 IRAEVEDNIMVTFKNLASRPYSFHSSLI----SYEEDQRAEPRG-----NFVQPGEVQTYSWKVLHQMAPTKQEFDCKAW 143

                          170       180
                   ....*....|....*....|....
gi 1131184096  503 PYYSNVDITRDLASGLIGLLLICK 526
Cdd:cd04228    144 AYFSNVDLEKDLHSGLIGPLIICK 167
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 352-527 2.71e-42

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


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 153.46  E-value: 2.71e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  352 YFIAAEEVIWDYAPIIPANMDKKYRSlhldnfsnRIGKhYKKVVYKQYQDDSFTKRleDPSSEGD---GILGPIIRAQVR 428
Cdd:cd14451      4 YYIAAEEEEWDYAGYGKSRLDKTQNE--------RDTV-FKKVVFRRYLDSTFSTP--DIQGEYEehlGILGPVIRAEVD 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  429 DTLKIVFKNMASRSYSIYPHGVTF------SPYDNEvnSSSASGSNTmirAVRPGETYTYKWNILESDEPTENDAQCLTR 502
Cdd:cd14451     73 DVIQVFFKNLASRPYSLHAHGLSYekssegLSYDDE--SPDWFKKDD---AVQPNGTYTYVWYANPRSGPENNGSDCRTW 147

                          170       180
                   ....*....|....*....|....*
gi 1131184096  503 PYYSNVDITRDLASGLIGLLLICKS 527
Cdd:cd14451    148 AYYSAVNPEKDIHSGLIGPLLICRK 172
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1486-1654 2.96e-42

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: 153.34  E-value: 2.96e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1486 YYIAAEEISWDY--SKFVQSDDIDYVPEDTV------------YKKVVFRKYLDSTFTKLDPQgeyEEHLGILGPVIRAE 1551
Cdd:cd04229      3 YYIAAEEVDWDYapSGKNKCCLGDDLEVSTLdsqpgpytigstYTKARYREYTDNSFSTPKPT---PAYLGILGPVIRAE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1552 VDDVIQVRFKN-LASRPYSLHAHGLSYEKSSEGKTYEDDSPewfkednaIQPNKTYTYVWHATTRSGPENPGSACRAWAY 1630
Cdd:cd04229     80 VGDTIKVVFKNnLDEFPVNMHPHGGLYSKDNEGTTDGAGDV--------VAPGETYTYRWIVPEDAGPGPGDPSSRLWLY 151

                          170       180
                   ....*....|....*....|....
gi 1131184096 1631 YSAVNPEKDIHSGLIGPLLICRKG 1654
Cdd:cd04229    152 HSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 351-526 6.46e-42

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: 151.94  E-value: 6.46e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  351 EYFIAAEEVIWDYAPiipanmdkKYRSLHLDNFsnriGKHYKKVVYKQYQDDsFTKrlEDPSSEGDGILGPIIRAQVRDT 430
Cdd:cd04226      2 EYYIAAQNIDWDYTP--------QSEELRLKRS----EQSFKKIVYREYEEG-FKK--EKPADLSSGLLGPTLRAEVGDT 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  431 LKIVFKNMASRSYSIYPHGVTFSPY-DNEVNSSSASGSNTMIRAVRPGETYTYKWNILESDEPTENDAQCLTRPYYSNVD 509
Cdd:cd04226     67 LIVHFKNMADKPLSIHPQGIAYGKKsEGSLYSDNTSPVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVN 146

                          170
                   ....*....|....*..
gi 1131184096  510 ITRDLASGLIGLLLICK 526
Cdd:cd04226    147 MVRDFNSGLIGALLICK 163
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 546-683 5.27e-40

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: 145.40  E-value: 5.27e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  546 VFAVFDENKSWYIEDNIYKFCENPEKVKRDDPKFYESNIMSTINGYVPESIPiLGFCFDDTVQWHFCSVGTQNDIFTIHF 625
Cdd:cd11016      7 LFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVFF 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1131184096  626 TGHSFIYGKRHEDTLTLFPMQGESVTVTMDNVGTWMLTTMNSNPRSKKLRLRFRDAKC 683
Cdd:cd11016     86 SGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1806-1961 1.77e-38

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


Pssm-ID: 214572  Cd Length: 139  Bit Score: 141.11  E-value: 1.77e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  1806 ECKMPMGLSTgliaDSQIQASEfwGYWEPKLARLNnGGSYNAWIAEKLStefnPEPWIQVDMQKEVLLTGIQTQGAKHyl 1885
Cdd:smart00231    1 PCNEPLGLES----DSQITASS--SYWAAKIARLN-GGSDGGWCPAKND----LPPWIQVDLGRLRTVTGVITGRRHG-- 67

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131184096  1886 KPYYTTEFCVaYSLDRKNWR*FKGnstRNVMYFGGNSDASTIKENQIDPPVVARYIRISPTGSYNKPALRLELQGC 1961
Cdd:smart00231   68 NGDWVTYKLE-YSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 32-196 3.94e-38

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 141.40  E-value: 3.94e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   32 RQFYVAAQSIRWNYRP------------ESTHLSSKPFETS----FKKIVYREY-EAYFQKEKPQSRTSGLLGPTLYAEV 94
Cdd:cd04229      1 RTYYIAAEEVDWDYAPsgknkcclgddlEVSTLDSQPGPYTigstYTKARYREYtDNSFSTPKPTPAYLGILGPVIRAEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   95 GDIMKVHFKNKAHK-PLSIHAQGIKYSKFSEGASysdhtlpmEKMDDAVAPGQEYTYEWIISEDSGPTHDDPPCLTHIYY 173
Cdd:cd04229     81 GDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTT--------DGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYH 152

                          170       180
                   ....*....|....*....|...
gi 1131184096  174 SYVNLVEDFNSGLIGPLLICKKG 196
Cdd:cd04229    153 SHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 351-526 5.82e-37

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


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 138.19  E-value: 5.82e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  351 EYFIAAEEVIWDYAPIIPANMDKKYRSlhldnFSNRIGKHYKKVVYKQYQDDSFTkrLEDPSSEGDGILGPIIRAQVRDT 430
Cdd:cd14452      2 RYYIAAVEIGWDYIHSDLGDPASEQRK-----KPKDIPQKYIKAVFVEYLDATFT--VPKPRPAWMGLLGPTIVAEVGDT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  431 LKIVFKNMASRSYSIYPHGVTF------SPYDNEVNSSSASGSntmirAVRPGETYTYKWNILESDEPTENDAQCLTRPY 504
Cdd:cd14452     75 VVITFKNLASQPYSLHAVGVSYwkasegAGYDDSTSQHEKEDD-----AVYPGGYHTYVWDISPKDGPTGSDPECLTYSY 149

                          170       180
                   ....*....|....*....|..
gi 1131184096  505 YSNVDITRDLASGLIGLLLICK 526
Cdd:cd14452    150 SSQVDPVKDVNSGLIGALLVCR 171
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1486-1653 8.26e-37

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: 137.75  E-value: 8.26e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1486 YYIAAEEISWDYSKFV-QSDDIDYVPE---------DTVYKKVVFRKYLDSTFTKldpQGEYEEHLGILGPVIRAEVDDV 1555
Cdd:cd04227      5 HYIAAEELDWDYAPLLsSTDDRELQSRylptgpqriGYKYKKVAFVEYTDKTFKR---REAKQTEKGILGPLLKGEVGDQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1556 IQVRFKNLASRPYSLHAHGLS------YEKSSEGKTYEDDSPewfkednaIQPNKTYTYVWHATTRSGPENPGSACRAWA 1629
Cdd:cd04227     82 IHIMFKNTASRPYNIYPHGLTsvrpmyRSRNPAGEKDLKTMP--------IGPGETFGYMWELTAEDGPTEEDPRCLTRL 153

                          170       180
                   ....*....|....*....|....
gi 1131184096 1630 YYSAVNPEKDIHSGLIGPLLICRK 1653
Cdd:cd04227    154 YQSTVDPERDLASGLIGPLLICKK 177
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1666-1802 1.39e-36

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: 135.78  E-value: 1.39e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1666 MREFVLLFMVFDEKKSWYYDKKPTRSWR---RASSE---VKNSHEFHAINGMIYN-LPGLRMYEQEWVRLHLLNLGGSRD 1738
Cdd:cd11018      1 VQEFALLFTIFDETKSWYFEENMRRNCRppcHIQTQdpwFHINNKFHAINGYVADtLPGLVMAQHQRIRWHLLNMGSDEE 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131184096 1739 IHVVHFHGQTLLENGTQQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLI 1802
Cdd:cd11018     81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 351-524 2.16e-36

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: 136.39  E-value: 2.16e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  351 EYFIAAEEVIWDYAPiipANMDK-------KYRSLHLDNFSNRIGKHYKKVVYKQYQDDSFTKRLEDPssEGDGILGPII 423
Cdd:cd04229      2 TYYIAAEEVDWDYAP---SGKNKcclgddlEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTP--AYLGILGPVI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  424 RAQVRDTLKIVFKN-MASRSYSIYPHGVtFSPYDNEVNSSSASGsntmirAVRPGETYTYKWNILESDEPTENDAQCLTR 502
Cdd:cd04229     77 RAEVGDTIKVVFKNnLDEFPVNMHPHGG-LYSKDNEGTTDGAGD------VVAPGETYTYRWIVPEDAGPGPGDPSSRLW 149

                          170       180
                   ....*....|....*....|..
gi 1131184096  503 PYYSNVDITRDLASGLIGLLLI 524
Cdd:cd04229    150 LYHSHVDVFAHTNAGLVGPIIV 171
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 32-195 5.25e-36

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: 135.29  E-value: 5.25e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   32 RQFYVAAQSIRWNYRPEST-----HLSSK-----PF--------ETSFKKIVYREY-EAYFQKekPQSRTS-----GLLG 87
Cdd:cd04225      1 RTYYIAAEEVEWDYSPQRTweqelHNTHEespgnAFlnkgdkfiGSKYKKVVYREYtDDTFSV--PKERTAeeehlGILG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   88 PTLYAEVGDIMKVHFKNKAHKPLSIHAQGIKYSkfsegasySDHTLPMEkmddavaPGQEYTYEWIISEDSGPTHDDPPC 167
Cdd:cd04225     79 PLIHAEVGEKVKIVFKNMASRPYSIHAHGVKTD--------SSWVAPTE-------PGETQTYTWKIPERSGPGVEDSNC 143

                          170       180
                   ....*....|....*....|....*...
gi 1131184096  168 LTHIYYSYVNLVEDFNSGLIGPLLICKK 195
Cdd:cd04225    144 ISWAYYSTVDQIKDLYSGLIGPLVICRR 171
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
 1965-2121 1.25e-35

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: 133.02  E-value: 1.25e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  1965 GCSTPLGMESgkieNKQITASSfkkswwgNYWEPFLARLNaQGHVNAWQAKANNNNQWLQIDLLKIKKITAIVTQGCKSL 2044
Cdd:smart00231    1 PCNEPLGLES----DSQITASS-------SYWAAKIARLN-GGSDGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHGN 68

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131184096  2045 SSEMYvksYTIHYSDQGTDWKPYREKSSMVdkiFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWNQSIALRLELFGC 2121
Cdd:smart00231   69 GDWVT---YKLEYSDDGVNWTTYKDGNSKV---FPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 34-195 2.62e-33

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: 127.74  E-value: 2.62e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   34 FYVAAQSIRWNYRP-----ESTHLSSKPFETS-------FKKIVYREYE-AYFQKEKPQSRTSGLLGPTLYAEVGDIMKV 100
Cdd:cd04227      5 HYIAAEELDWDYAPllsstDDRELQSRYLPTGpqrigykYKKVAFVEYTdKTFKRREAKQTEKGILGPLLKGEVGDQIHI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  101 HFKNKAHKPLSIHAQGI------KYSKFSEGASYSdHTLPmekmddaVAPGQEYTYEWIISEDSGPTHDDPPCLTHIYYS 174
Cdd:cd04227     85 MFKNTASRPYNIYPHGLtsvrpmYRSRNPAGEKDL-KTMP-------IGPGETFGYMWELTAEDGPTEEDPRCLTRLYQS 156

                          170       180
                   ....*....|....*....|.
gi 1131184096  175 YVNLVEDFNSGLIGPLLICKK 195
Cdd:cd04227    157 TVDPERDLASGLIGPLLICKK 177
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1981-2118 1.63e-32

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: 123.33  E-value: 1.63e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1981 QITASSfkkSWWGNYwePFLARLNaqGHVN-AWQAKANNNNQWLQIDLLKIKKITAIVTQGCKSLSSeMYVKSYTIHYSD 2059
Cdd:pfam00754    1 QITASS---SYSGEG--PAAAALD--GDPNtAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSN-GYVTSYKIEYSL 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131184096 2060 QGTDWKPYRekssmvDKIFEGNNNVRGHVKNFFNPPIISRFIRIIPKTWN--QSIALRLEL 2118
Cdd:pfam00754   73 DGENWTTVK------DEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNggNGIALRAEL 127
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 547-668 5.86e-32

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: 122.58  E-value: 5.86e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  547 FAVFDENKSWYIEDNIYKFCENPEKVKRDDPKFYESNIMSTINGYVPESIPILGFCFDDTVQWHFCSVGTQNDIFTIHFT 626
Cdd:cd11021      8 FSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHSAFFH 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1131184096  627 GHSFIYGKRHEDTLTLFPMQGESVTVTMDNVGTWMLTTMNSN 668
Cdd:cd11021     88 GQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVND 129
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 547-683 3.58e-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: 120.28  E-value: 3.58e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  547 FAVFDENKSWYIEDNIYKFCENPEKVKRDDPKFYESNIMSTINGYVPESIPILGFCFDDTVQWHFCSVGTQNDIFTIHFT 626
Cdd:cd11022      8 FTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVHGIYFS 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131184096  627 GHSFIYGKRHEDTLTLFPMQgeSVTVTM--DNVGTWMLTTMNSNPRSKKLRLRFRDAKC 683
Cdd:cd11022     88 GNTFLLQGTRRDTANLFPHT--SVTAIMqpDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 32-196 6.37e-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: 117.68  E-value: 6.37e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   32 RQFYVAAQSIRWNY---------RPESTHLSSKPFETSFKKIVYREY--EAYFQkekPQSRTS-----GLLGPTLYAEVG 95
Cdd:cd04228      2 RHYFIAAVEVLWDYgmqrpqhflRARDPNRGRRKSVPQYKKVVFREYldGSFTQ---PVYRGEldehlGILGPYIRAEVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   96 DIMKVHFKNKAHKPLSIHAQGIKYskfsEGASYSDHtlpmekMDDAVAPGQEYTYEWIISEDSGPTHDDPPCLTHIYYSY 175
Cdd:cd04228     79 DNIMVTFKNLASRPYSFHSSLISY----EEDQRAEP------RGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSN 148

                          170       180
                   ....*....|....*....|.
gi 1131184096  176 VNLVEDFNSGLIGPLLICKKG 196
Cdd:cd04228    149 VDLEKDLHSGLIGPLIICKTG 169
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1668-1803 5.84e-27

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: 108.42  E-value: 5.84e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1668 EFVLLFMVFDEKKSWY-------YDKKPTRSwRRASSEVKNSHEFHAINGMIY-NLPGLRMYEQEWVRLHLLNLGGSRDI 1739
Cdd:cd11012      3 EFALLFLVFDENESWYldeniktYSDHPEKV-NKEDEEFIESNKMHAINGKVFgNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131184096 1740 HVVHFHGQTLLENGTQQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLIV 1803
Cdd:cd11012     82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 208-326 2.32e-26

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: 106.40  E-value: 2.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  208 EKQHVLMFAVFDESKSWN----------------------QTSSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPE 265
Cdd:cd11021      1 DREFVLMFSVVDENLSWYldeniktycsepakvdkddedfQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131184096  266 LFTIHFNGQVLEQNHHKISAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDI 326
Cdd:cd11021     81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1667-1800 2.68e-26

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: 106.40  E-value: 2.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1667 REFVLLFMVFDEKKSWYYDKKPTRSWRRASSEVKNSHEF------HAINGMIY-NLPGLRMYEQEWVRLHLLNLGGSRDI 1739
Cdd:cd11021      2 REFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFqesnkmHSINGYTFgNLPGLSMCAGDRVKWHLFGMGNEVDI 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131184096 1740 HVVHFHGQTLLENGtqqHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPF 1800
Cdd:cd11021     82 HSAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFY 139
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 546-662 5.52e-26

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: 105.72  E-value: 5.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  546 VFAVFDENKSWYIEDNIYKFCENPEKVKRDDPKFYESNIMSTINGYVPESIPILGFCFDDTVQWHFCSVGTQNDIFTIHF 625
Cdd:cd11012      7 LFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHTAHF 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1131184096  626 TGHSFIY---GKRHEDTLTLFPMQGESVTVTMDNVGTWML 662
Cdd:cd11012     87 HGHSFDYkhrGVYRSDVFDLFPGTFQTVEMIPRTPGTWLL 126
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
 1822-1958 8.53e-26

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


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 104.45  E-value: 8.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1822 QIQASEFWGYWEPKLARLNNGGSyNAWIaeklSTEFNPEPWIQVDMQKEVLLTGIQTQGAKHyLKPYYTTEFCVAYSLDR 1901
Cdd:pfam00754    1 QITASSSYSGEGPAAAALDGDPN-TAWS----AWSGDDPQWIQVDLGKPKKITGVVTQGRQD-GSNGYVTSYKIEYSLDG 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131184096 1902 KNWR*FKGNSTRnvmyfgGNSDASTIKENQIDPPVVARYIRISPTG--SYNKPALRLEL 1958
Cdd:pfam00754   75 ENWTTVKDEKIP------GNNDNNTPVTNTFDPPIKARYVRIVPTSwnGGNGIALRAEL 127
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 209-326 1.47e-24

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: 101.14  E-value: 1.47e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  209 KQHVLMFAVFDESKSW--NQTSSL-------------MYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPELFTIHFNG 273
Cdd:cd11015      2 QAFVLLFAVFDEGKSWysEVGERKsrdkfkradsrkeFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFFEG 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1131184096  274 QVLEQNHHKISAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDI 326
Cdd:cd11015     82 HTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 547-662 5.26e-23

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: 96.87  E-value: 5.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  547 FAVFDENKSWYIEDNIYKFCENPEKVKRDDPKFYESNIMSTINGYVPESIPILGFCFDDTVQWHFCSVGTQNDIFTIHFT 626
Cdd:cd11018      8 FTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHSVHFH 87

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1131184096  627 GHSFIYGKRHEDTL---TLFPMQGESVTVTMDNVGTWML 662
Cdd:cd11018     88 GLPFTVRAKKEYRMgvyNLYPGVFGTVEMRPSTAGIWLV 126
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1667-1802 9.88e-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: 89.96  E-value: 9.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1667 REFVLLFMVFDEKKSWYYDKKPTRSWRRASSEvKNSHEFHAINGMI-YNLPGLRMYEQEWVRLHLLNLGGSRDIHVVHFH 1745
Cdd:cd11015      2 QAFVLLFAVFDEGKSWYSEVGERKSRDKFKRA-DSRKEFHTINGYInASLPGLKICQRKPVIWHVIGMGTAPEVHSIFFE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131184096 1746 GQTLLengTQQHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLI 1802
Cdd:cd11015     81 GHTFL---VRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1667-1802 6.39e-20

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 87.28  E-value: 6.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1667 REFVLLFMVFDEKkswyydkkptrswrrassEVKNSHEFHAINGMIY-NLPGLRMYEQEWVRLHLLNLGGSRDIHVVHFH 1745
Cdd:cd11023      2 QEFIENSSIFLDL------------------NVEEAGLMHSINGYVFgNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWH 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131184096 1746 GQTLLENGTQQHQlgVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLI 1802
Cdd:cd11023     64 GQTVEADKSRRTD--VAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1667-1796 7.67e-20

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: 87.92  E-value: 7.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1667 REFVLLFMVFDEKKSWYYDKKPTRSWRRASSEVKNSHEF------HAINGMIY-NLPGLRMYEQEWVRLHLLNLGGSRDI 1739
Cdd:cd11022      2 KEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFqesnkmHSINGYMYgNQPGLDMCKGDTVSWHLFGLGTETDV 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1131184096 1740 HVVHFHGQTLLENGTQQHQLGvwpLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGM 1796
Cdd:cd11022     82 HGIYFSGNTFLLQGTRRDTAN---LFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGM 135
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1667-1797 2.18e-17

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 80.29  E-value: 2.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1667 REFVLLFMVFDEKKSWYydkkptrswrraSSEVKNSHEFHAINGMIY-NLPGLRMYEQEWVRLHLLNLGGSRDIHVVHFH 1745
Cdd:cd14453      2 KEYVLMFGVFDENKSWY------------KQNASVDSVKYTINGYTNgTLPDVSICAYDHVSWHLLGMSSEPELFSVHFN 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1131184096 1746 GQTLLENGtqqHQLGVWPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQ 1797
Cdd:cd14453     70 GQVLEQNG---HKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMY 118
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 208-329 8.87e-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: 79.06  E-value: 8.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  208 EKQHVLMFAVFDESKSWN----------------------QTSSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPE 265
Cdd:cd11022      1 DKEFFLLFTVFDENESWYldeniqqftldprsvdkededfQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131184096  266 LFTIHFNGQVLEQNHHKISAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDIKNC 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 ...
 542-665 4.36e-15

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


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 73.74  E-value: 4.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  542 EQQAV--FAVFDENKSWYiedniykfcenpekvkRDDPKfyESNIMSTINGYVPESIPILGFCFDDTVQWHFCSVGTQND 619
Cdd:cd14453      1 YKEYVlmFGVFDENKSWY----------------KQNAS--VDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1131184096  620 IFTIHFTGHSFIYGKRHEDTLTLfpMQGESVTVTMDNV--GTWMLTTM 665
Cdd:cd14453     63 LFSVHFNGQVLEQNGHKVSAVGL--VSGSSTTASMTVVhtGRWLISSL 108
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 213-322 6.59e-15

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: 73.76  E-value: 6.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  213 LMFAVFDESKSWNQTSSL----------------------MYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPELFTIH 270
Cdd:cd11018      6 LLFTIFDETKSWYFEENMrrncrppchiqtqdpwfhinnkFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHSVH 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1131184096  271 FNGQVL---EQNHHKISAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQA 322
Cdd:cd11018     86 FHGLPFtvrAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSA 140
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 547-664 1.82e-13

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: 69.51  E-value: 1.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  547 FAVFDENKSWYIEDNIYKFCEnpeKVKRDDPKFYESNIMSTINGyVPESIPILGFCFDDTVQWHFCSVGTQNDIFTIHFT 626
Cdd:cd14455      8 FMTFDEEKSWYYEKNRKRTCR---ENRVKDPNVQDNHTFHAING-IIYNLKGLRMYTNELVRWHLINMGGPKDLHVVHFH 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1131184096  627 GHSFIYGKRHEDTLTLFP-MQGESVTVTM--DNVGTWMLTT 664
Cdd:cd14455     84 GQTFTEKGLKDHQLGVYPlLPGSFATLEMkpSKPGLWLLET 124
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 546-670 4.94e-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: 4.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  546 VFAVFDENKSWYiedniykfCENPEKVKRDDPKFYESNI-MSTINGYVPESIPILGFCFDDTVQWHFCSVGTQNDIFTIH 624
Cdd:cd11015      7 LFAVFDEGKSWY--------SEVGERKSRDKFKRADSRKeFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIF 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1131184096  625 FTGHSFIYGKRHEDTLTLFPMQGESVTVTMDNVGTWMLTTMNSNPR 670
Cdd:cd11015     79 FEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQ 124
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1537-1651 8.60e-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: 66.93  E-value: 8.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1537 YEEHLGILGPVIRAEVDDVIQVRFKN-LASRPYSLHAHGLSYEKSSEGktyedDSPEWFKEDnAIQPNKTYTYVWHATTR 1615
Cdd:cd04206     22 ITVNGQFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDG-----DGVAGLTQC-PIPPGESFTYRFTVDDQ 95

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1131184096 1616 SGpenpgsacrAWAYYSAVNPEKDihSGLIGPLLIC 1651
Cdd:cd04206     96 AG---------TFWYHSHVGGQRA--DGLYGPLIVE 120
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 84-193 6.35e-12

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: 64.23  E-value: 6.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   84 GLLGPTLYAEVGDIMKVHFKNK-AHKPLSIHAQGIkyskFSEGASYSDHTLPMEKmdDAVAPGQEYTYEWIISEDSGpth 162
Cdd:cd04206     27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGL----RQPGTNDGDGVAGLTQ--CPIPPGESFTYRFTVDDQAG--- 97

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1131184096  163 ddppclTHIYYSYVNLveDFNSGLIGPLLIC 193
Cdd:cd04206     98 ------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 215-320 7.44e-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: 64.17  E-value: 7.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  215 FAVFDESKswNQTSSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPELFTIHFNGQVLEQNHHKISAI-TLISATS 293
Cdd:cd11023      8 SSIFLDLN--VEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRTDVaELMPASM 85

                           90       100
                   ....*....|....*....|....*..
gi 1131184096  294 TTANMTVSPEGRWTIASLIPRHFQAGM 320
Cdd:cd11023     86 RVADMTAADVGTWLLHCHVHDHYMAGM 112
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 87-153 1.70e-11

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: 63.06  E-value: 1.70e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131184096   87 GPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIKYSKFsegasysDHTLPMEkmddaVAPGQEYTYEWI 153
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAM-------DGTGLGP-----IMPGESFTYEFV 86
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 208-329 3.07e-11

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: 63.35  E-value: 3.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  208 EKQHVLMFAVFDESKSWN----------------------QTSSLMYTVNGYVNGTMpDITVCAHDHISWHLIGMSSGPE 265
Cdd:cd11016      1 DKDWSLLFSVFDENNSWYlkenihrftqtpagvndtdpdfYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131184096  266 LFTIHFNGQVLEQNHHKISAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQAYIDIKNC 329
Cdd:cd11016     80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1670-1802 5.68e-11

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: 62.58  E-value: 5.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1670 VLLFMVFDEKKSWYYDKKPTRSWRRASS------EVKNSHEFHAINGMIYNLPGLRMYEQEWVRLHLLNLGGSRDIHVVH 1743
Cdd:cd11016      5 SLLFSVFDENNSWYLKENIHRFTQTPAGvndtdpDFYASNVMHTINGIVFDRRQFVICLTDVAYWYVLSVGAQTDFLSVF 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131184096 1744 FHGQTLLENGTQQHQLgvwPLLPGSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLI 1802
Cdd:cd11016     85 FSGNTFKHQMVYEDVL---TLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTV 140
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 208-311 8.22e-11

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: 62.20  E-value: 8.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  208 EKQHVLMFAVFDESKSWNQ----------------------TSSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPE 265
Cdd:cd14454      1 DLEQHAVFAVFDENKSWYLeeninkycsnpnnvkkddpkfyKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1131184096  266 LFTIHFNGQVLEQNHHKISAITLISATSTTANMTVSPEGRWTIASL 311
Cdd:cd14454     81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSF 126
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 581-662 4.93e-10

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: 59.16  E-value: 4.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  581 ESNIMSTINGYVPESIPILGFCFDDTVQWHFCSVGTQNDIFTIHFTGHSFIYGK-RHEDTLTLFPMQGESVTVTMDNVGT 659
Cdd:cd11023     18 EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKsRRTDVAELMPASMRVADMTAADVGT 97


                   ...
gi 1131184096  660 WML 662
Cdd:cd11023     98 WLL 100
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 209-322 5.86e-10

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: 59.50  E-value: 5.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  209 KQHVLMFAVFDESKSW-------------------NQT---SSLMYTVNGYVNGTMPDITVCAHDHISWHLIGMSSGPEL 266
Cdd:cd11012      2 LEFALLFLVFDENESWyldeniktysdhpekvnkeDEEfieSNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1131184096  267 FTIHFNGQVLEQNH---HKISAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQA 322
Cdd:cd11012     82 HTAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMET 140
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 209-322 1.51e-09

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: 58.34  E-value: 1.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  209 KQHVLMFAVFDESKSWN-------------------QTSSLMYTVNGYVNgTMPDITVCAHDHISWHLIGMSSGPELFTI 269
Cdd:cd14455      2 REFVLLFMTFDEEKSWYyeknrkrtcrenrvkdpnvQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHVV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131184096  270 HFNGQVLEQN---HHKISAITLISATSTTANMTVSPEGRWTIASLIPRHFQAGMQA 322
Cdd:cd14455     81 HFHGQTFTEKglkDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQT 136
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 416-525 4.65e-09

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


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 56.14  E-value: 4.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  416 DGILGPIIRAQVRDTLKIVFKN-MASRSYSIYPHGVTF--SPYDNEVNSSSASgsntmirAVRPGETYTYKWNIlesdep 492
Cdd:cd04206     26 GQFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQpgTNDGDGVAGLTQC-------PIPPGESFTYRFTV------ 92

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1131184096  493 tenDAQCLTRPYYSNVDITRdlASGLIGLLLIC 525
Cdd:cd04206     93 ---DDQAGTFWYHSHVGGQR--ADGLYGPLIVE 120
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1543-1737 1.06e-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: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1543 ILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGL--SYEkssegktyEDDSPEwfkedNAIQPNKTYTYVWHATTRSG--- 1617
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLrvPNA--------MDGVPG-----DPIAPGETFTYEFPVPQPAGtyw 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1618 --PENPGSacrawayySAVNpekdIHSGLIGPLLIcrkgtLDKETNMPVDMREFVLLF--MVFDEKKSWYYDkkptrswr 1693
Cdd:COG2132    109 yhPHTHGS--------TAEQ----VYRGLAGALIV-----EDPEEDLPRYDRDIPLVLqdWRLDDDGQLLYP-------- 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1131184096 1694 RASSEVKNSHEFHAINGMIynLPGLRMYEQEWVRLHLLNLGGSR 1737
Cdd:COG2132    164 MDAAMGGRLGDTLLVNGRP--NPTLEVRPGERVRLRLLNASNAR 205
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 87-192 2.31e-08

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: 54.19  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   87 GPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIkyskFSEGASYSDHTLPMekMDDAVAPGQEYTYEWIISEDSGpthddpp 166
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGL----FQNGTNWMDGTAGI--TQCPIPPGGSFTYNFTVDGQYG------- 96

                           90       100
                   ....*....|....*....|....*..
gi 1131184096  167 clTHIYYS-YVNLVEDfnsGLIGPLLI 192
Cdd:cd13857     97 --TYWYHShYSTQYAD---GLVGPLIV 118
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 84-192 4.08e-08

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: 53.39  E-value: 4.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   84 GLLGPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIKyskfsegasysdhtLPmEKMD-------DAVAPGQEYTYEWIIsE 156
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLR--------------LP-NAMDgvpgltqPPVPPGESFTYEFTP-P 91

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1131184096  157 DSGpthddppclTHIYYSYVNLVEDFNSGLIGPLLI 192
Cdd:cd13861     92 DAG---------TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1672-1807 6.84e-08

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: 53.72  E-value: 6.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1672 LFMVFDEKKSWYYDKKPTRSWRRASSEVKNSHEF------HAINGMIY-NLPGLRMYEQEWVRLHLLNLGGSRDIHVVHF 1744
Cdd:cd14454      7 VFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFyksnimPTINGYAYeSSAPLGFCHSEVVQWHISSVGTQDEIITVHL 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131184096 1745 HGQTLLENGTQQHQLGVWPLlpgSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLivDREC 1807
Cdd:cd14454     87 SGHTFRYKGKHEDTLNLFPM---SGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFT--DVIC 144
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1545-1653 1.09e-07

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 52.65  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1545 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTyeddspewfKEDNAIQPNKTYTYVW--HATTR--SGPEN 1620
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG---------MNASIVAPGDTRIYTWrtHGGYRraDGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1131184096 1621 PGSAcRAWAYYSAV----NPEKDIHSGLIGPLLICRK 1653
Cdd:cd14449    100 EGTA-GYWHYHDHVfgteHGTEGLSRGLYGALIVRRV 135
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1083-1400 1.38e-07

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 56.85  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1083 DQTSPNDTTSqTSSPPDLYPT---VSPEEHYQIFPIQDSDPTHSTTAPSNRSPDPTHSTTAPS-NRSPP----TQPSQIP 1154
Cdd:pfam05109  505 DMTSPTSAVT-TPTPNATSPTpavTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTpNATIPtlgkTSPTSAV 583

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1155 NYDLRNRAIPTdVSQIFPSlelevwQTATSLDLSQPSISPdlgqMALSPdPGQESLSPDLGQTSL-SPDLSQESLSPDLG 1233
Cdd:pfam05109  584 TTPTPNATSPT-VGETSPQ------ANTTNHTLGGTSSTP----VVTSP-PKNATSAVTTGQHNItSSSTSSMSLRPSSI 651

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1234 QTALSPDPSQESLSPDLGQTSLSPDlGQESLSPDLGQTALSPDPSQESLSPDLGQTSLSPDLGQTALSPDPSQESL---S 1310
Cdd:pfam05109  652 SETLSPSTSDNSTSHMPLLTSAHPT-GGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVtkgT 730

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1311 PDLGQTSLSPDLGQESLSPDLGQTALSPDLSL----------ESLSPDLSQLDLKQTSPPLDLNQTSHTSESSQSLPLPE 1380
Cdd:pfam05109  731 PPKNATSPQAPSGQKTAVPTVTSTGGKANSTTggkhttghgaRTSTEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPR 810

                          330       340
                   ....*....|....*....|.
gi 1131184096 1381 FGQTFPNADIGQMPSP-PPDS 1400
Cdd:pfam05109  811 WTFTSPPVTTAQATVPvPPTS 831
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1076-1383 4.32e-07

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 55.31  E-value: 4.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1076 AASLPDHDQTSPNDTTSqTSSPPDLYPTV---SPEEHYQIFPIQDSDPTHSTTAPSNRSPDPTHSTTAPS--------NR 1144
Cdd:pfam05109  512 AVTTPTPNATSPTPAVT-TPTPNATSPTLgktSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTsavttptpNA 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1145 SPPTQPSQIPNYDLRNRAIPTDVSQifPSLELEVWQTATSLDLSQPSI-SPDLGQMALSPDPGQESLSPDLGQTSLSPDL 1223
Cdd:pfam05109  591 TSPTVGETSPQANTTNHTLGGTSST--PVVTSPPKNATSAVTTGQHNItSSSTSSMSLRPSSISETLSPSTSDNSTSHMP 668

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1224 SQESLSPDLGQTALSPDP--------SQESLSPDLGQTSLSPDLGQESLSPDLGQTALSP-DPSQESLSPDL--GQTSLS 1292
Cdd:pfam05109  669 LLTSAHPTGGENITQVTPaststhhvSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKgTPPKNATSPQApsGQKTAV 748

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1293 PDLGQTALSPDPSQ--ESLSPDLGQTSLSP--DLGQESLSPDL---GQTALSPDLSlESLSPDLSqldlkQTSPPLDLNQ 1365
Cdd:pfam05109  749 PTVTSTGGKANSTTggKHTTGHGARTSTEPttDYGGDSTTPRTrynATTYLPPSTS-SKLRPRWT-----FTSPPVTTAQ 822

                          330
                   ....*....|....*...
gi 1131184096 1366 TshtsessqSLPLPEFGQ 1383
Cdd:pfam05109  823 A--------TVPVPPTSQ 832
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 87-192 9.97e-07

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: 9.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   87 GPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIkyskfsegasysdhTLPMEkMD-------DAVAPGQEYTYEWIIsEDSG 159
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGL--------------PVPNG-MDgvpgitqPPIQPGETFTYEFTA-KQAG 94

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1131184096  160 pthddppclTHIYYSYVNLVEDFNSGLIGPLLI 192
Cdd:cd13860     95 ---------TYMYHSHVDEAKQEDMGLYGAFIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 85-192 1.03e-06

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: 49.55  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   85 LLGPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIKYSK--FSEGASYSDHtlpmekmdDAVAPGQEYTYEWIISEDSGpth 162
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGtpWMDGVPGVTQ--------CPIPPGQSFTYRFQVKQQAG--- 92

                           90       100       110
                   ....*....|....*....|....*....|
gi 1131184096  163 ddppclTHIYYSYVNLVEdfNSGLIGPLLI 192
Cdd:pfam07732   93 ------TYWYHSHTSGQQ--AAGLAGAIII 114
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 87-192 2.93e-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: 2.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   87 GPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIKYSKFSEGASysdhtlpMEKMDdaVAPGQEYTYEW----IISEDSGPTH 162
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG-------MNASI--VAPGDTRIYTWrthgGYRRADGSWA 99

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1131184096  163 DDPPCLTHiYYSYV----NLVEDFNSGLIGPLLI 192
Cdd:cd14449    100 EGTAGYWH-YHDHVfgteHGTEGLSRGLYGALIV 132
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1072-1413 3.35e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.46  E-value: 3.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1072 NLSLAASLPD-HDQTSPNDTTSQT----SSPPDLYPTVSPeehyqifPIQDSDPTHSTTAPSNRSPDPTHSTTAPSNRSP 1146
Cdd:pfam03154  141 NRSTSPSIPSpQDNESDSDSSAQQqilqTQPPVLQAQSGA-------ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPA 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1147 PTQPSQIPNYDLrnraiptdvsqifPSLELeVWQTATSLDLSQPSISPDLGQMALSPDPGQ---ESLSPDLGQTSLSPDL 1223
Cdd:pfam03154  214 TSQPPNQTQSTA-------------APHTL-IQQTPTLHPQRLPSPHPPLQPMTQPPPPSQvspQPLPQPSLHGQMPPMP 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1224 SQESLSPDLGQTALSPDP------SQESLSPDLGQTSLSPDLGQESLSPDLGQTALSPDPSQESLSP--DLGQTSLSPDl 1295
Cdd:pfam03154  280 HSLQTGPSHMQHPVPPQPfpltpqSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPpaPLSMPHIKPP- 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1296 GQTALSPDPSQESLSPDLGQTSLSPDLGQESLSPdlgQTALSPDLSLESLSPDLSQldlkqtSPPLDLNQTSHTSES--- 1372
Cdd:pfam03154  359 PTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPP---PPALKPLSSLSTHHPPSAH------PPPLQLMPQSQQLPPppa 429

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1131184096 1373 -------SQSLPlPEFGQTFPNADIGQMPSPPPdstlnntFKPEEFNP 1413
Cdd:pfam03154  430 qppvltqSQSLP-PPAASHPPTSGLHQVPSQSP-------FPQHPFVP 469
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 85-247 3.68e-06

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: 51.86  E-value: 3.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   85 LLGPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIkyskfsegasysdhTLPMEkMD----DAVAPGQEYTYEWIIsedsgp 160
Cdd:COG2132     42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL--------------RVPNA-MDgvpgDPIAPGETFTYEFPV------ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  161 thDDPPClTHIYYSYVNLVEDFN--SGLIGPLLIckkgtltEDGTQKM--FEKQHVLMFAvfDesKSWNQTSSLMYTVNG 236
Cdd:COG2132    101 --PQPAG-TYWYHPHTHGSTAEQvyRGLAGALIV-------EDPEEDLprYDRDIPLVLQ--D--WRLDDDGQLLYPMDA 166

                          170
                   ....*....|..
gi 1131184096  237 YVNGTMPD-ITV 247
Cdd:COG2132    167 AMGGRLGDtLLV 178
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1051-1398 6.81e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.71  E-value: 6.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1051 LLHASNETSLSIDLNQTFPSMNLSLAASLPDHDQTSPndTTSQTSSPPDLYPTVSPEEHYQIFPIQDSDPTHSTTAPSNR 1130
Cdd:PHA03307    35 LLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGP--PPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPS 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1131 SPDPTHSTTAPSNRSPPTQPSQIPNYDLRNRAIPTDV-SQIFPSLELEVWQ--TATSLDLSQPSISPDlgQMALSPDPGQ 1207
Cdd:PHA03307   113 SPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAaSPPAAGASPAAVAsdAASSRQAALPLSSPE--ETARAPSSPP 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1208 ESLSPDLGQTSLSPDLSqeSLSPDLGQTALSPDPSQESLSPDLGQTSLSPDLGQESLSPDLGQTALSPDPsqeslSPDLG 1287
Cdd:PHA03307   191 AEPPPSTPPAAASPRPP--RRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLP-----RPAPI 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1288 QTSLSPDLGQTALSPDPSQESLSPDLGQTSLSPDlgQESLSPDLGQTALSPDLSLESLSPDLSQLDLKQTSPPLDLNQTS 1367
Cdd:PHA03307   264 TLPTRIWEASGWNGPSSRPGPASSSSSPRERSPS--PSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAV 341

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1131184096 1368 HTSESSQSLPLPefGQTFPNADigqmPSPPP 1398
Cdd:PHA03307   342 SPGPSPSRSPSP--SRPPPPAD----PSSPR 366
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1069-1413 1.93e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1069 PSMNLSLAASLPDHDQTSPNDTTSQTSSPPDL-----YPTVSPEEHYQIFPIQDSDPTHSTTAPSNRSPDPTHSTTAPSN 1143
Cdd:PHA03247  2551 PPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVtsrarRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS 2630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1144 RSP-------PTQPSQIPNYDLRNRAIPTDVS--QIFPSLELEVWQTATSLDLSQPSISPDLGQMALSPDPGQESLSPDL 1214
Cdd:PHA03247  2631 PSPaanepdpHPPPTVPPPERPRDDPAPGRVSrpRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEP 2710

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1215 GQTSLSPDL-------SQESLSPDLGQTALSPDPSQESLSPDLGQTSLSPDLGQESLS------PDLGQTALSPDPSQES 1281
Cdd:PHA03247  2711 APHALVSATplppgpaAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPApappaaPAAGPPRRLTRPAVAS 2790

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1282 LSPDLGQTSLSPDLGQTALSPDPSQESLSPDLG-QTSLSPDLGQESLSPDLGQTALSPDLSLE-SLSP--DLSQLDLKQT 1357
Cdd:PHA03247  2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASpAGPLPPPTSAQPTAPPPPPGPPPPSLPLGgSVAPggDVRRRPPSRS 2870

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1131184096 1358 SPPLDLNQTSHTSESSQSLPLPEFGQTFPNADIGQMPSPPPDSTLNNTFKPEEFNP 1413
Cdd:PHA03247  2871 PAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPP 2926
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 420-484 2.06e-05

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 46.11  E-value: 2.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131184096  420 GPIIRAQVRDTLKIVFKNMASRSYSIYPHGVtfspyDNEVNSSSASGSNTmirAVRPGETYTYKW 484
Cdd:cd14449     29 GPVIEVREGDTLKILFRNTLDVPASLHPHGV-----DYTTASDGTGMNAS---IVAPGDTRIYTW 85
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1080-1410 2.32e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 2.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1080 PDHDQTSPNDTTSQTSSPPDLYPTVSPEEHYQIFPIQDSDPTHSTTAPSNRSPDPTHSTTAPSNRSPPTQPSQIPnydlR 1159
Cdd:PHA03247  2705 PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP----P 2780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1160 NRAIPTDVSQIFPSLElevwqtatslDLSQPSISPDLGQMALSPDPGQ-ESLSPdlgQTSLSPDLSQESLSPdlgqtALS 1238
Cdd:PHA03247  2781 RRLTRPAVASLSESRE----------SLPSPWDPADPPAAVLAPAAALpPAASP---AGPLPPPTSAQPTAP-----PPP 2842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1239 PDPSQESLSPdlgQTSLSPDlGQESLSPDLGQTALSPDPSQESLSPDLGQTSLSPDLGQTALSPDPSQESLSPDLGQTSL 1318
Cdd:PHA03247  2843 PGPPPPSLPL---GGSVAPG-GDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1319 ----------------SPDLGQESLSPDLGQTALS------PDLSLESLSPDLSQLDLKQTSPPLDLNQTSHTSESS-QS 1375
Cdd:PHA03247  2919 pqpqpppppqpqppppPPPRPQPPLAPTTDPAGAGepsgavPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPlTG 2998

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1131184096 1376 LPLPEFGQTFPNADIGQMPSPPPDSTLNNTFKPEE 1410
Cdd:PHA03247  2999 HSLSRVSSWASSLALHEETDPPPVSLKQTLWPPDD 3033
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1545-1617 2.53e-05

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: 45.37  E-value: 2.53e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131184096 1545 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLsyekSSEGKTYEDDSP---EWfkednAIQPNKTYTYVWHATTRSG 1617
Cdd:cd13850     28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPWSDGVPgvtQW-----PIQPGGSFTYRWKAEDQYG 94
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 1092-1350 2.76e-05

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 49.15  E-value: 2.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1092 SQTSSPPDLYPTVSPEEHYQIFPIQDSDPTHSTTAPSNRSPdpthsTTAPSNRSPPTQPSQIPNYDLRNRAIPTDVSQIF 1171
Cdd:PLN03209   333 SDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSP-----YTAYEDLKPPTSPIPTPPSSSPASSKSVDAVAKP 407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1172 PSLELE-VWQTATSLDLSQPSISPDLGQMALSPDPGQESLSPdlgQTSLSPDlsqeslspdlGQTALSPDPSQESLSPDL 1250
Cdd:PLN03209   408 AEPDVVpSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKP---PTSPSPT----------APTGVSPSVSSTSSVPAV 474

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1251 GQTSLSPDLGQESLSPDLGQTALSPDPSQESLSPdlgQTSLSPDLGQTALSPDPSQESLSPDLGQTSLSPDLGQESLSPD 1330
Cdd:PLN03209   475 PDTAPATAATDAAAPPPANMRPLSPYAVYDDLKP---PTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPK 551

                          250       260
                   ....*....|....*....|
gi 1131184096 1331 lgQTALSPDLSLESLSPDLS 1350
Cdd:PLN03209   552 --PRPLSPYTMYEDLKPPTS 569
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 420-524 3.72e-05

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 44.95  E-value: 3.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  420 GPIIRAQVRDTLKIVFKNMASRSYSIYPHGVtfspYDNEVNSSSASgsntmirAVRPGETYTYKWnilesdeptenDAQC 499
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGI----HDAAMDGTGLG-------PIMPGESFTYEF-----------VAEP 89

                           90       100
                   ....*....|....*....|....*..
gi 1131184096  500 L-TRPYYSNV-DITRDLASGLIGLLLI 524
Cdd:cd11024     90 AgTHLYHCHVqPLKEHIAMGLYGAFIV 116
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 1542-1650 4.00e-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: 44.92  E-value: 4.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1542 GILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPewfkednaIQPNKTYTYvwhattRSGPENP 1621
Cdd:cd13861     28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGLTQPP--------VPPGESFTY------EFTPPDA 93

                           90       100
                   ....*....|....*....|....*....
gi 1131184096 1622 GSACrawaYYSAVNPEKDIHSGLIGPLLI 1650
Cdd:cd13861     94 GTYW----YHPHVGSQEQLDRGLYGPLIV 118
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 420-484 4.25e-05

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: 45.16  E-value: 4.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1131184096  420 GPIIRAQVRDTLKIVFKNMASRSYSIYPHGVTfspydnEVNSSSASG-SNTMIRAVRPGETYTYKW 484
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVL------QMGSWKMDGvPGVTQPAIEPGESFTYKF 90
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1085-1342 4.43e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 4.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1085 TSPNDTTSQTSSPPDLYPTVSPEEHYQ--IFPIQD-----------SDPTHSTTAPSNRSPDPTHSTTAPSNRSPPTQPS 1151
Cdd:PHA03247  2827 PLPPPTSAQPTAPPPPPGPPPPSLPLGgsVAPGGDvrrrppsrspaAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE 2906

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1152 QIPNYDLRNRAIPTDVSQIFPSLELEVWQTAtsldLSQPSISPDlGQMALSPDPGQESLSPDLGQTSLS----PDLSQES 1227
Cdd:PHA03247  2907 RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP----RPQPPLAPT-TDPAGAGEPSGAVPQPWLGALVPGrvavPRFRVPQ 2981

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1228 LSPDLGQTALSPDPSQESLSPDLGQTSLSPDLGQESLSP--DLGQTALSPDPSQESlSPDLGQTSLSPDLGQTALSPDPS 1305
Cdd:PHA03247  2982 PAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPpvSLKQTLWPPDDTEDS-DADSLFDSDSERSDLEALDPLPP 3060

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1131184096 1306 QESLSPDLGQTSLSPDLG-QESLSPDLGQTALSPDLSL 1342
Cdd:PHA03247  3061 EPHDPFAHEPDPATPEAGaRESPSSQFGPPPLSANAAL 3098
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1545-1650 4.83e-05

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


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 44.57  E-value: 4.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1545 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSyekssegKTYEDDSpewFKEDnaIQPNKTYTYVWHAttrsgpENPGsa 1624
Cdd:cd11024     32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIH-------DAAMDGT---GLGP--IMPGESFTYEFVA------EPAG-- 91

                           90       100
                   ....*....|....*....|....*..
gi 1131184096 1625 crAWAYYSAVNPEKD-IHSGLIGPLLI 1650
Cdd:cd11024     92 --THLYHCHVQPLKEhIAMGLYGAFIV 116
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 1545-1650 8.13e-05

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: 44.01  E-value: 8.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1545 GPVIRA-EVDDVIqVRFKNLASRPYSLHAHGLsYEKSSegkTYEDDSPEWFKEdnAIQPNKTYTYVWHAttrsgpENPGS 1623
Cdd:cd13859     31 GPLIHVkEGDDLV-VHVTNNTTLPHTIHWHGV-LQMGS---WKMDGVPGVTQP--AIEPGESFTYKFKA------ERPGT 97

                           90       100
                   ....*....|....*....|....*...
gi 1131184096 1624 acrAWaYYSAVN-PEKDIHSGLIGPLLI 1650
Cdd:cd13859     98 ---LW-YHCHVNvNEHVGMRGMWGPLIV 121
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 1545-1650 1.87e-04

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


Pssm-ID: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 43.02  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1545 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLsYEkssEGKTYEDDSPEWfkEDNAIQPNKTYTYVWHATTRSGPenpgsa 1624
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGL-FQ---NGTNWMDGTAGI--TQCPIPPGGSFTYNFTVDGQYGT------ 97

                           90       100
                   ....*....|....*....|....*...
gi 1131184096 1625 crAW--AYYSAVNPEkdihsGLIGPLLI 1650
Cdd:cd13857     98 --YWyhSHYSTQYAD-----GLVGPLIV 118
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 87-159 2.43e-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: 42.63  E-value: 2.43e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131184096   87 GPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIK--YSKFSEGASYSDHTlPMEkmddavaPGQEYTYEWIISEDSG 159
Cdd:cd13849     28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRqlRSGWADGPAYITQC-PIQ-------PGQSYTYRFTVTGQEG 94
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1707-1783 3.24e-04

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 42.26  E-value: 3.24e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131184096 1707 AINGMIynlPG--LRMYEQEWVRLHLLNLGgsRDIHVVHFHGQtlleNGTQQHQLGVWPLLPGSFKTLEMKASKPGWWL 1783
Cdd:cd11024     25 TYNGTV---PGptLRATEGDLVRIHFINTG--DHPHTIHFHGI----HDAAMDGTGLGPIMPGESFTYEFVAEPAGTHL 94
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 1545-1650 3.28e-04

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: 42.18  E-value: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1545 GPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSsegktyEDDSPEwfKEDNAIQPNKTYTYVWHATtrsgpeNPGSa 1624
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNG------MDGVPG--ITQPPIQPGETFTYEFTAK------QAGT- 95

                           90       100
                   ....*....|....*....|....*.
gi 1131184096 1625 craWAYYSAVNPEKDIHSGLIGPLLI 1650
Cdd:cd13860     96 ---YMYHSHVDEAKQEDMGLYGAFIV 118
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 420-524 7.70e-04

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


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 41.28  E-value: 7.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  420 GPIIRAQVRDTLKIVFKN-MASRSYSIYPHGV--TFSPYDNEVNSSSASgsntmirAVRPGETYTYKWNIlesDEPTend 496
Cdd:cd13845     30 GPTIRATAGDTIVVELENkLPTEGVAIHWHGIrqRGTPWADGTASVSQC-------PINPGETFTYQFVV---DRPG--- 96

                           90       100
                   ....*....|....*....|....*...
gi 1131184096  497 aqclTRPYYSNVDITRdlASGLIGLLLI 524
Cdd:cd13845     97 ----TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 1710-1780 8.72e-04

Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles two domain nitrite reductase in both sequence homology and structure similarity. It consists of two domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of larger laccases.


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 41.32  E-value: 8.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131184096 1710 GMIYN--LPG--LRMYEQEWVRLHLLNLGGSRDIHVVHFHGQTllengTQQHQLGVWPLLPGSFKTLEMKASKPG 1780
Cdd:cd04201     23 YWTFDgdIPGpmLRVREGDTVELHFSNNPSSTMPHNIDFHAAT-----GAGGGAGATFIAPGETSTFSFKATQPG 92
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1543-1617 1.09e-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: 40.69  E-value: 1.09e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131184096 1543 ILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSegktYEDDSPEWfkEDNAIQPNKTYTYVWHATTRSG 1617
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTP----WMDGVPGV--TQCPIPPGQSFTYRFQVKQQAG 92
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 420-524 1.66e-03

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: 40.26  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  420 GPIIRAQVRDTLKIVFKNMASRSYSIYPHGVtfsPYDNEVNSssASGSNTmiRAVRPGETYTYKWNILESDeptendaqc 499
Cdd:cd13860     31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGL---PVPNGMDG--VPGITQ--PPIQPGETFTYEFTAKQAG--------- 94

                           90       100
                   ....*....|....*....|....*
gi 1131184096  500 lTRPYYSNVDITRDLASGLIGLLLI 524
Cdd:cd13860     95 -TYMYHSHVDEAKQEDMGLYGAFIV 118
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 587-669 1.70e-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: 40.76  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  587 TINGYVPESIPILGFCFDDTVQWHFCSVGTqNDIFTIHFTGHSFIY----GKRHE----DTLTLFPMQGESVTVTMDN-V 657
Cdd:pfam00394   40 LINGKDGASLATLTVTPGKTYRLRIINVAL-DDSLNFSIEGHKMTVvevdGVYVNpftvDSLDIFPGQRYSVLVTANQdP 118

                           90
                   ....*....|..
gi 1131184096  658 GTWMLTTMNSNP 669
Cdd:pfam00394  119 GNYWIVASPNIP 130
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1534-1618 1.88e-03

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.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 39.91  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1534 QGEYEEHLGILGPVIRAEVDDVIQVRFKNLASRPYSLHAHGLsyekssEGKT--YEDDSPEWFKEDNAIQPNKTYTYVWH 1611
Cdd:cd00920     11 SFTYNGVLLFGPPVLVVPVGDTVRVQFVNKLGENHSVTIAGF------GVPVvaMAGGANPGLVNTLVIGPGESAEVTFT 84


                   ....*..
gi 1131184096 1612 aTTRSGP 1618
Cdd:cd00920     85 -TDQAGV 90
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1705-1806 2.11e-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: 40.50  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1705 FHAINGMIY--NLPGLRMYEQEWVRLHLLNLGGsrDIHVVHFHGQT--LLENGTQQHQL----------GVW----PLLP 1766
Cdd:pfam07731   21 DWAINGLLFppNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSfqVLGRGGGPWPEedpktynlvdPVRrdtvQVPP 98

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1131184096 1767 GSFKTLEMKASKPGWWLLDTEVGEIQRAGMQTPFLIVDRE 1806
Cdd:pfam07731   99 GGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 87-192 3.00e-03

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: 39.77  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   87 GPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIkyskFSEGASYSDHTLPMEKmdDAVAPGQEYTYEWiISEDSGpthddpp 166
Cdd:cd13859     31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGV----LQMGSWKMDGVPGVTQ--PAIEPGESFTYKF-KAERPG------- 96

                           90       100
                   ....*....|....*....|....*..
gi 1131184096  167 clTHIYYSYVNLVE-DFNSGLIGPLLI 192
Cdd:cd13859     97 --TLWYHCHVNVNEhVGMRGMWGPLIV 121
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 84-162 3.93e-03

The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs 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: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 39.38  E-value: 3.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131184096   84 GLLGPTLYAEVGDIMKVHFKNKAHKPLSIHAQGIKYSKFSEGAsysdhtlPMekmdDAVAPGQEYTYEWIISEDSGPTH 162
Cdd:cd13855     29 SVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGN-------PH----DPVAPGNDRVYRFTLPQDSAGTY 96
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 1527-1617 5.10e-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: 38.79  E-value: 5.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1527 TFTKLDPQGEYEEH-LGILG----PVIRAEVDDVIQVRFKN-LASRPYSLHAHGLsYEKSsegkTYEDDSPEWFKEdNAI 1600
Cdd:cd13851      8 TWVTANPDGLFERRvIGINGqwppPPIEVNKGDTVVIHATNsLGDQPTSLHFHGL-FQNG----TNYMDGPVGVTQ-CPI 81

                           90
                   ....*....|....*..
gi 1131184096 1601 QPNKTYTYVWHATTRSG 1617
Cdd:cd13851     82 PPGQSFTYEFTVDTQVG 98
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 420-524 5.18e-03

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: 38.78  E-value: 5.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096  420 GPIIRAQVRDTLKIVFKNMASRSYSIYPHGVTF--SPYDNEVNSSSASGsntmiraVRPGETYTYKWNIlesdeptenDA 497
Cdd:cd13857     30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQngTNWMDGTAGITQCP-------IPPGGSFTYNFTV---------DG 93

                           90       100
                   ....*....|....*....|....*..
gi 1131184096  498 QCLTRPYYSNVDITrdLASGLIGLLLI 524
Cdd:cd13857     94 QYGTYWYHSHYSTQ--YADGLVGPLIV 118
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1707-1800 5.28e-03

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


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 39.37  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1707 AINGMIY-----NLPGLRMYEQEWVRLHLLNLGGSRDIHVVHFHG---QTLLENGTQQHQL-----GVW----PLLPGSF 1769
Cdd:cd04207     21 VINGMPFkegdaNTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGhsfWVLGSGGGPFDAPlnltnPPWrdtvLVPPGGW 100

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1131184096 1770 KTLEMKASKPGWWLLDTEVGEIQRAGMQTPF 1800
Cdd:cd04207    101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVF 131
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 1519-1613 6.17e-03

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: 38.76  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1519 VFRKY-LDSTFTKLDPQGEYEEHLGILG----PVIRAEVDDVIQVRFKN-LASRPYSLHAHGLSyeksSEGKTYEDDSP- 1591
Cdd:cd13854      2 VTRKYtLTITNSTLAPDGVEKEVMLINGqypgPLIEANWGDTIEVTVINkLQDNGTSIHWHGIR----QLNTNWQDGVPg 77

                           90       100
                   ....*....|....*....|....
gi 1131184096 1592 --EWfkednAIQPNKTYTYVWHAT 1613
Cdd:cd13854     78 vtEC-----PIAPGDTRTYRFRAT 96
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 418-486 6.27e-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: 38.77  E-value: 6.27e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131184096  418 ILGPIIRAQVRDTLKIVFKNMASRSYSIYPHG--VTFSPYDNEVNsssaSGSNTMIravRPGETYTYKWNI 486
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGlqQRGTPWMDGVP----GVTQCPI---PPGQSFTYRFQV 87
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 88-192 8.10e-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: 38.40  E-value: 8.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096   88 PTLYAEVGDIMKVHFKNK-AHKPLSIHAQGIkyskFSEGASYsdhtlpmekMDDAV-------APGQEYTYEWIISEDSG 159
Cdd:cd13851     32 PPIEVNKGDTVVIHATNSlGDQPTSLHFHGL----FQNGTNY---------MDGPVgvtqcpiPPGQSFTYEFTVDTQVG 98

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1131184096  160 pthddppclTHIYYSYVNlvEDFNSGLIGPLLI 192
Cdd:cd13851     99 ---------TYWYHSHDG--GQYPDGLRGPFII 120
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 1667-1784 8.93e-03

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


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 38.77  E-value: 8.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131184096 1667 REFVllfMVFDEkkswyYDKKPTRSWRRASSEVKNsheFHAINGMIY-NLPGLRMYEQEWVRLHLLNLggSRDIHVVHFH 1745
Cdd:cd04202      2 RDYT---LVLQE-----WFVDPGTTPMPPEGMDFN---YFTINGKSFpATPPLVVKEGDRVRIRLINL--SMDHHPMHLH 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1131184096 1746 GQTLL---ENGTQQHQLGVWPL-----LPGSFKTLEMKASKPGWWLL 1784
Cdd:cd04202     69 GHFFLvtaTDGGPIPGSAPWPKdtlnvAPGERYDIEFVADNPGDWMF 115
 
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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