NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1777334|dbj|BAA12207|]
View 

Bf/C2 [Oryzias latipes]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 252-450 4.99e-95

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


:

Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 293.42  E-value: 4.99e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  252 LNIYIALDISESVEEEHFKRAKLAIITLIKKIAAFTVSPNYEILFFSADVYEVVSIVEFYEGKITleSAIKNLEDFQIGD 331
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDAD--DVIKRLEDFNYDD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  332 KS--TGTDVNAALKKFEEGMAWIEQKTGDKFSEHRHVFLLFTDGAYNMGGSPLPTLARIKNRVYMSPTGDpGSRLDYLES 409
Cdd:cd01470  79 HGdkTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSD-NPREDYLDV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 1777334  410 YVFGIGANIFDDDLLPLTAGTEGELHYFRLKKETNLAATFD 450
Cdd:cd01470 158 YVFGVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 474-705 1.39e-36

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


:

Pssm-ID: 214473  Cd Length: 229  Bit Score: 137.42  E-value: 1.39e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334     474 KDGKRRRYPWVVFINIQGKSPKkCLGSLVSSEFVLTAAHCFIfSDEPQDVKV-----EIDDGKGSKEKKVKTFKLHPQYN 548
Cdd:smart00020   6 SEANIGSFPWQVSLQYGGGRHF-CGGSLISPRWVLTAAHCVR-GSDPSNIRVrlgshDLSSGEEGQVIKVSKVIIHPNYN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334     549 vtarvkqgvAEFYDYDIALIQLERPVQLSISARPICIPCTKETsdalrLPGSATCRDQEELLLKNQRERLSfltrteplV 628
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYN-----VPAGTTCTVSGWGRTSEGAGSLP--------D 141

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777334     629 GEKDVYAKLGDNRDlCIKKAlkakgitttDPKVPVTDNFLCTGG-DRDHIACTGDSGGAVFKNYEsRTIQIALVSWGT 705
Cdd:smart00020 142 TLQEVNVPIVSNAT-CRRAY---------SGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWGS 208
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 89-144 1.22e-16

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 74.42  E-value: 1.22e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334   89 CPDPNVLENGNVFPPLERYLAGNTTTFECYSGYTMRGSSSRTCLSNGKWSGSTTIC 144
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 152-205 2.61e-10

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 56.32  E-value: 2.61e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334  152 CPDPGVPPGASRRG--NTFDVGYDVTYSCNGNLFLVGSRVRVCQENSQWTGREPAC 205
Cdd:cd00033   1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 252-450 4.99e-95

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 293.42  E-value: 4.99e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  252 LNIYIALDISESVEEEHFKRAKLAIITLIKKIAAFTVSPNYEILFFSADVYEVVSIVEFYEGKITleSAIKNLEDFQIGD 331
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDAD--DVIKRLEDFNYDD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  332 KS--TGTDVNAALKKFEEGMAWIEQKTGDKFSEHRHVFLLFTDGAYNMGGSPLPTLARIKNRVYMSPTGDpGSRLDYLES 409
Cdd:cd01470  79 HGdkTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSD-NPREDYLDV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 1777334  410 YVFGIGANIFDDDLLPLTAGTEGELHYFRLKKETNLAATFD 450
Cdd:cd01470 158 YVFGVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 474-705 1.39e-36

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 137.42  E-value: 1.39e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334     474 KDGKRRRYPWVVFINIQGKSPKkCLGSLVSSEFVLTAAHCFIfSDEPQDVKV-----EIDDGKGSKEKKVKTFKLHPQYN 548
Cdd:smart00020   6 SEANIGSFPWQVSLQYGGGRHF-CGGSLISPRWVLTAAHCVR-GSDPSNIRVrlgshDLSSGEEGQVIKVSKVIIHPNYN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334     549 vtarvkqgvAEFYDYDIALIQLERPVQLSISARPICIPCTKETsdalrLPGSATCRDQEELLLKNQRERLSfltrteplV 628
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYN-----VPAGTTCTVSGWGRTSEGAGSLP--------D 141

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777334     629 GEKDVYAKLGDNRDlCIKKAlkakgitttDPKVPVTDNFLCTGG-DRDHIACTGDSGGAVFKNYEsRTIQIALVSWGT 705
Cdd:smart00020 142 TLQEVNVPIVSNAT-CRRAY---------SGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWGS 208
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 474-738 1.99e-36

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 137.02  E-value: 1.99e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  474 KDGKRRRYPWVVFINIQGKSpKKCLGSLVSSEFVLTAAHCFIfSDEPQDVKV------EIDDGKGSKEKKVKTFKLHPQY 547
Cdd:cd00190   5 SEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY-SSAPSNYTVrlgshdLSSNEGGGQVIKVKKVIVHPNY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  548 NVTarvkqgvaeFYDYDIALIQLERPVQLSISARPICIPCTKETsdalrLPGSATCR-----DQEELLLKNQRERlsflt 622
Cdd:cd00190  83 NPS---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCTvsgwgRTSEGGPLPDVLQ----- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  623 rteplvgekDVYAKLGDNRDlCIKKalkakgittTDPKVPVTDNFLCTGGDR-DHIACTGDSGGAVFKNYESRTIQIALV 701
Cdd:cd00190 144 ---------EVNVPIVSNAE-CKRA---------YSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIV 204

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 1777334  702 SWGTQeiCTGGGMrettPesrDFHINLFKMVPFLKSI 738
Cdd:cd00190 205 SWGSG--CARPNY----P---GVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
481-713 6.90e-24

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 100.59  E-value: 6.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    481 YPWVVFINIQGKSPKkCLGSLVSSEFVLTAAHCFifsDEPQDVKVEIDD------GKGSKEKKVKTFKLHPQYNvtarvk 554
Cdd:pfam00089  12 FPWQVSLQLSSGKHF-CGGSLISENWVLTAAHCV---SGASDVKVVLGAhnivlrEGGEQKFDVEKIIVHPNYN------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    555 qgvAEFYDYDIALIQLERPVQLSISARPICIPctkeTSDALRLPGSaTCrdqeellLKNQRERLSFLTRTEPL-VGEKDV 633
Cdd:pfam00089  82 ---PDTLDNDIALLKLESPVTLGDTVRPICLP----DASSDLPVGT-TC-------TVSGWGNTKTLGPSDTLqEVTVPV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    634 YaklgdNRDLCikkalkakgitTTDPKVPVTDNFLCTG-GDRDhiACTGDSGGAVFKNyesRTIQIALVSWGTQeiCTGG 712
Cdd:pfam00089 147 V-----SRETC-----------RSAYGGTVTDTMICAGaGGKD--ACQGDSGGPLVCS---DGELIGIVSWGYG--CASG 203


                  .
gi 1777334    713 G 713
Cdd:pfam00089 204 N 204
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 481-713 3.80e-22

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 96.64  E-value: 3.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  481 YPWVVFI-NIQGKSPKKCLGSLVSSEFVLTAAHCfIFSDEPQDVKVEID----DGKGSKEKKVKTFKLHPQYNVTArvkq 555
Cdd:COG5640  42 YPWMVALqSSNGPSGQFCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGstdlSTSGGTVVKVARIVVHPDYDPAT---- 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  556 gvaefYDYDIALIQLERPVQlsiSARPICIPctkETSDALRlPGS--------ATCRDQEElllknQRERLsfLTRTEPL 627
Cdd:COG5640 117 -----PGNDIALLKLATPVP---GVAPAPLA---TSADAAA-PGTpatvagwgRTSEGPGS-----QSGTL--RKADVPV 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  628 VGEKDVYAKLGDNrdlcikkalkakgitttdpkvpvTDNFLCTGGDR-DHIACTGDSGGAVFKNYESRTIQIALVSWGTQ 706
Cdd:COG5640 178 VSDATCAAYGGFD-----------------------GGTMLCAGYPEgGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGG 234


                ....*..
gi 1777334  707 EiCTGGG 713
Cdd:COG5640 235 P-CAAGY 240
VWA pfam00092
von Willebrand factor type A domain;
253-451 1.13e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 92.72  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    253 NIYIALDISESVEEEHFKRAKLAIITLIKKIAAFTVSPNYEILFFSADVYEVVSIVEfYEGKITLESAIKNLEDFQIGDK 332
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLND-YSSKEELLSAVDNLRYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    333 STGTDVNAALKKFEEGMAWIEqktgdkfSEHRHVFLLFTDGaYNMGGSPLPTLARIKNRVYmsptgdpgsrldylESYVF 412
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGAR-------PGAPKVVVLLTDG-RSQDGDPEEVARELKSAGV--------------TVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1777334    413 GIGANifDDDLLPLTAGTEGELHYFRLKKETNLAATFDD 451
Cdd:pfam00092 138 GVGNA--DDEELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 253-454 1.21e-18

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 84.04  E-value: 1.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334     253 NIYIALDISESVEEEHFKRAKLAIITLIKKIAAFTVSPNYEILFFSADVYEVVSiVEFYEGKITLESAIKNLEDFQIGDK 332
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFP-LNDSRSKDALLEALASLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334     333 STGTDVNAALKKFEEGMAwieqktgDKFSEHRHVFLLFTDGAYNMGGSPLPTLARIKNRvymsptgdpgsrlDYLESYVF 412
Cdd:smart00327  80 NLGAALQYALENLFSKSA-------GSRRGAPKVVILITDGESNDGPKDLLKAAKELKR-------------SGVKVFVV 139

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1777334     413 GIGANiFDDDLLPLTAGTEGELHYFrlkketnLAATFDDIID 454
Cdd:smart00327 140 GVGND-VDEEELKKLASAPGGVYVF-------LPELLDLLID 173
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 89-144 1.22e-16

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 74.42  E-value: 1.22e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334   89 CPDPNVLENGNVFPPLERYLAGNTTTFECYSGYTMRGSSSRTCLSNGKWSGSTTIC 144
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 89-144 1.98e-15

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 71.02  E-value: 1.98e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334      89 CPDPNVLENGNVFPPLERYLAGNTTTFECYSGYTMRGSSSRTCLSNGKWSGSTTIC 144
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
89-144 3.20e-12

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 61.75  E-value: 3.20e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334     89 CPDPNVLENGNVFPPLERYLAGNTTTFECYSGYTMRGSSSRTCLSNGKWSGSTTIC 144
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 152-205 2.61e-10

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 56.32  E-value: 2.61e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334  152 CPDPGVPPGASRRG--NTFDVGYDVTYSCNGNLFLVGSRVRVCQENSQWTGREPAC 205
Cdd:cd00033   1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 41-205 2.66e-10

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 61.59  E-value: 2.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    41 GLETNSLLVYQCPDNFYPYPDTIRVCHPNKQ----WKPRpkkfSPQrCKPVECPDPNVLENGNVFPPLERYLAGNTTTFE 116
Cdd:PHA02927 101 GVDFGSSITYSCNSGYQLIGESKSYCELGSTgsmvWNPE----API-CESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334   117 CYSGYTMRGSSSRTClSNGKWSGSTTiCSRDSgdaCPDPGVPPGASRRG--NTFDVGYDVTYSCNGNLFLVGSRVRVCQE 194
Cdd:PHA02927 176 CNSGYSLIGNSGVLC-SGGEWSDPPT-CQIVK---CPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSP 250

                        170
                 ....*....|.
gi 1777334   195 NSQWTGREPAC 205
Cdd:PHA02927 251 GNTWQPELPKC 261
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 152-205 1.09e-09

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 54.84  E-value: 1.09e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334     152 CPDPGVPPGASRRG--NTFDVGYDVTYSCNGNLFLVGSRVRVCQENSQWTGREPAC 205
Cdd:smart00032   1 CPPPPDIENGTVTSssGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
152-205 7.11e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.42  E-value: 7.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334    152 CPDPGVPPGA--SRRGNTFDVGYDVTYSCNGNLFLVGSRVRVCQENSQWTGREPAC 205
Cdd:pfam00084   1 CPPPPDIPNGkvSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 227-452 5.15e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 51.86  E-value: 5.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  227 DSLTTLQPTNDTQAGRKIRISKNGTLNIYIALDISESVEEEH-FKRAKLAIITLIKKIAAFTvspNYEILFFSADVYEVV 305
Cdd:COG1240  68 LLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLL 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  306 SIVEfyegkiTLESAIKNLEDFQIGDkstGTDVNAALkkfEEGMAWIEQKTGDKfseHRHVFLLfTDGAYNMGGSPLPTL 385
Cdd:COG1240 145 PLTR------DREALKRALDELPPGG---GTPLGDAL---ALALELLKRADPAR---RKVIVLL-TDGRDNAGRIDPLEA 208

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1777334  386 AR-IKNRvymsptgdpGSRLdylesYVFGIGANIFDDDLLP-LTAGTEGElhYFRLKKETNLAATFDDI 452
Cdd:COG1240 209 AElAAAA---------GIRI-----YTIGVGTEAVDEGLLReIAEATGGR--YFRADDLSELAAIYREI 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 46-146 2.49e-05

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 46.57  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    46 SLLVYQCPDNFYPYPDTIRVChPNKQWKprpkkfSPQRCKPVECPDPNVLeNGNVFPPLER-YLAGNTTTFECYSGYTMR 124
Cdd:PHA02927 170 SVVTYSCNSGYSLIGNSGVLC-SGGEWS------DPPTCQIVKCPHPTIS-NGYLSSGFKRsYSYNDNVDFKCKYGYKLS 241

                         90       100
                 ....*....|....*....|..
gi 1777334   125 GSSSRTCLSNGKWSGSTTICSR 146
Cdd:PHA02927 242 GSSSSTCSPGNTWQPELPKCVR 263
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 252-450 4.99e-95

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 293.42  E-value: 4.99e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  252 LNIYIALDISESVEEEHFKRAKLAIITLIKKIAAFTVSPNYEILFFSADVYEVVSIVEFYEGKITleSAIKNLEDFQIGD 331
Cdd:cd01470   1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDAD--DVIKRLEDFNYDD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  332 KS--TGTDVNAALKKFEEGMAWIEQKTGDKFSEHRHVFLLFTDGAYNMGGSPLPTLARIKNRVYMSPTGDpGSRLDYLES 409
Cdd:cd01470  79 HGdkTGTNTAAALKKVYERMALEKVRNKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSD-NPREDYLDV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 1777334  410 YVFGIGANIFDDDLLPLTAGTEGELHYFRLKKETNLAATFD 450
Cdd:cd01470 158 YVFGVGDDVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 474-705 1.39e-36

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 137.42  E-value: 1.39e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334     474 KDGKRRRYPWVVFINIQGKSPKkCLGSLVSSEFVLTAAHCFIfSDEPQDVKV-----EIDDGKGSKEKKVKTFKLHPQYN 548
Cdd:smart00020   6 SEANIGSFPWQVSLQYGGGRHF-CGGSLISPRWVLTAAHCVR-GSDPSNIRVrlgshDLSSGEEGQVIKVSKVIIHPNYN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334     549 vtarvkqgvAEFYDYDIALIQLERPVQLSISARPICIPCTKETsdalrLPGSATCRDQEELLLKNQRERLSfltrteplV 628
Cdd:smart00020  84 ---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYN-----VPAGTTCTVSGWGRTSEGAGSLP--------D 141

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777334     629 GEKDVYAKLGDNRDlCIKKAlkakgitttDPKVPVTDNFLCTGG-DRDHIACTGDSGGAVFKNYEsRTIQIALVSWGT 705
Cdd:smart00020 142 TLQEVNVPIVSNAT-CRRAY---------SGGGAITDNMLCAGGlEGGKDACQGDSGGPLVCNDG-RWVLVGIVSWGS 208
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 474-738 1.99e-36

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 137.02  E-value: 1.99e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  474 KDGKRRRYPWVVFINIQGKSpKKCLGSLVSSEFVLTAAHCFIfSDEPQDVKV------EIDDGKGSKEKKVKTFKLHPQY 547
Cdd:cd00190   5 SEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY-SSAPSNYTVrlgshdLSSNEGGGQVIKVKKVIVHPNY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  548 NVTarvkqgvaeFYDYDIALIQLERPVQLSISARPICIPCTKETsdalrLPGSATCR-----DQEELLLKNQRERlsflt 622
Cdd:cd00190  83 NPS---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCTvsgwgRTSEGGPLPDVLQ----- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  623 rteplvgekDVYAKLGDNRDlCIKKalkakgittTDPKVPVTDNFLCTGGDR-DHIACTGDSGGAVFKNYESRTIQIALV 701
Cdd:cd00190 144 ---------EVNVPIVSNAE-CKRA---------YSYGGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIV 204

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 1777334  702 SWGTQeiCTGGGMrettPesrDFHINLFKMVPFLKSI 738
Cdd:cd00190 205 SWGSG--CARPNY----P---GVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
481-713 6.90e-24

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 100.59  E-value: 6.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    481 YPWVVFINIQGKSPKkCLGSLVSSEFVLTAAHCFifsDEPQDVKVEIDD------GKGSKEKKVKTFKLHPQYNvtarvk 554
Cdd:pfam00089  12 FPWQVSLQLSSGKHF-CGGSLISENWVLTAAHCV---SGASDVKVVLGAhnivlrEGGEQKFDVEKIIVHPNYN------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    555 qgvAEFYDYDIALIQLERPVQLSISARPICIPctkeTSDALRLPGSaTCrdqeellLKNQRERLSFLTRTEPL-VGEKDV 633
Cdd:pfam00089  82 ---PDTLDNDIALLKLESPVTLGDTVRPICLP----DASSDLPVGT-TC-------TVSGWGNTKTLGPSDTLqEVTVPV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    634 YaklgdNRDLCikkalkakgitTTDPKVPVTDNFLCTG-GDRDhiACTGDSGGAVFKNyesRTIQIALVSWGTQeiCTGG 712
Cdd:pfam00089 147 V-----SRETC-----------RSAYGGTVTDTMICAGaGGKD--ACQGDSGGPLVCS---DGELIGIVSWGYG--CASG 203


                  .
gi 1777334    713 G 713
Cdd:pfam00089 204 N 204
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 252-437 2.60e-23

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 96.98  E-value: 2.60e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  252 LNIYIALDISESVEEEHFKRAKLAIITLIKKIAAFTVSPNYEILFFSADVYEVVSIVEfYEGKITLESAIKNLEDfqigD 331
Cdd:cd01450   1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLND-YKSKDDLLKAVKNLKY----L 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  332 KSTGTDVNAALKKFEEGMAwieqKTGDKFSEHRHVFLLFTDGAYNMGGSPLPTLARIKNRvymsptgdpgsrldYLESYV 411
Cdd:cd01450  76 GGGGTNTGKALQYALEQLF----SESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE--------------GIKVFV 137

                       170       180
                ....*....|....*....|....*.
gi 1777334  412 FGIGAniFDDDLLPLTAGTEGELHYF 437
Cdd:cd01450 138 VGVGP--ADEEELREIASCPSERHVF 161
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 481-713 3.80e-22

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 96.64  E-value: 3.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  481 YPWVVFI-NIQGKSPKKCLGSLVSSEFVLTAAHCfIFSDEPQDVKVEID----DGKGSKEKKVKTFKLHPQYNVTArvkq 555
Cdd:COG5640  42 YPWMVALqSSNGPSGQFCGGTLIAPRWVLTAAHC-VDGDGPSDLRVVIGstdlSTSGGTVVKVARIVVHPDYDPAT---- 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  556 gvaefYDYDIALIQLERPVQlsiSARPICIPctkETSDALRlPGS--------ATCRDQEElllknQRERLsfLTRTEPL 627
Cdd:COG5640 117 -----PGNDIALLKLATPVP---GVAPAPLA---TSADAAA-PGTpatvagwgRTSEGPGS-----QSGTL--RKADVPV 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  628 VGEKDVYAKLGDNrdlcikkalkakgitttdpkvpvTDNFLCTGGDR-DHIACTGDSGGAVFKNYESRTIQIALVSWGTQ 706
Cdd:COG5640 178 VSDATCAAYGGFD-----------------------GGTMLCAGYPEgGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGG 234


                ....*..
gi 1777334  707 EiCTGGG 713
Cdd:COG5640 235 P-CAAGY 240
VWA pfam00092
von Willebrand factor type A domain;
253-451 1.13e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 92.72  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    253 NIYIALDISESVEEEHFKRAKLAIITLIKKIAAFTVSPNYEILFFSADVYEVVSIVEfYEGKITLESAIKNLEDFQIGDK 332
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLND-YSSKEELLSAVDNLRYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    333 STGTDVNAALKKFEEGMAWIEqktgdkfSEHRHVFLLFTDGaYNMGGSPLPTLARIKNRVYmsptgdpgsrldylESYVF 412
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGAR-------PGAPKVVVLLTDG-RSQDGDPEEVARELKSAGV--------------TVFAV 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1777334    413 GIGANifDDDLLPLTAGTEGELHYFRLKKETNLAATFDD 451
Cdd:pfam00092 138 GVGNA--DDEELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 253-454 1.21e-18

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 84.04  E-value: 1.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334     253 NIYIALDISESVEEEHFKRAKLAIITLIKKIAAFTVSPNYEILFFSADVYEVVSiVEFYEGKITLESAIKNLEDFQIGDK 332
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFP-LNDSRSKDALLEALASLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334     333 STGTDVNAALKKFEEGMAwieqktgDKFSEHRHVFLLFTDGAYNMGGSPLPTLARIKNRvymsptgdpgsrlDYLESYVF 412
Cdd:smart00327  80 NLGAALQYALENLFSKSA-------GSRRGAPKVVILITDGESNDGPKDLLKAAKELKR-------------SGVKVFVV 139

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1777334     413 GIGANiFDDDLLPLTAGTEGELHYFrlkketnLAATFDDIID 454
Cdd:smart00327 140 GVGND-VDEEELKKLASAPGGVYVF-------LPELLDLLID 173
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 89-144 1.22e-16

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 74.42  E-value: 1.22e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334   89 CPDPNVLENGNVFPPLERYLAGNTTTFECYSGYTMRGSSSRTCLSNGKWSGSTTIC 144
Cdd:cd00033   1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 89-144 1.98e-15

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 71.02  E-value: 1.98e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334      89 CPDPNVLENGNVFPPLERYLAGNTTTFECYSGYTMRGSSSRTCLSNGKWSGSTTIC 144
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
89-144 3.20e-12

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 61.75  E-value: 3.20e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334     89 CPDPNVLENGNVFPPLERYLAGNTTTFECYSGYTMRGSSSRTCLSNGKWSGSTTIC 144
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 252-387 6.24e-12

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 64.51  E-value: 6.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  252 LNIYIALDISESVEEEHFKRAKLAIITLIKKIAAFTVSPNYEILFFSADVYEVVSIVEFYEgKITLESAIKNLEDFQIGd 331
Cdd:cd00198   1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTD-KADLLEAIDALKKGLGG- 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334  332 kstGTDVNAALKKFeegmawIEQKTGDKFSEHRHVFLLFTDGAYNMGGSPLPTLAR 387
Cdd:cd00198  79 ---GTNIGAALRLA------LELLKSAKRPNARRVIILLTDGEPNDGPELLAEAAR 125
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 152-205 2.61e-10

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 56.32  E-value: 2.61e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334  152 CPDPGVPPGASRRG--NTFDVGYDVTYSCNGNLFLVGSRVRVCQENSQWTGREPAC 205
Cdd:cd00033   1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 41-205 2.66e-10

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 61.59  E-value: 2.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    41 GLETNSLLVYQCPDNFYPYPDTIRVCHPNKQ----WKPRpkkfSPQrCKPVECPDPNVLENGNVFPPLERYLAGNTTTFE 116
Cdd:PHA02927 101 GVDFGSSITYSCNSGYQLIGESKSYCELGSTgsmvWNPE----API-CESVKCQSPPSISNGRHNGYEDFYTDGSVVTYS 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334   117 CYSGYTMRGSSSRTClSNGKWSGSTTiCSRDSgdaCPDPGVPPGASRRG--NTFDVGYDVTYSCNGNLFLVGSRVRVCQE 194
Cdd:PHA02927 176 CNSGYSLIGNSGVLC-SGGEWSDPPT-CQIVK---CPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSP 250

                        170
                 ....*....|.
gi 1777334   195 NSQWTGREPAC 205
Cdd:PHA02927 251 GNTWQPELPKC 261
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 152-205 1.09e-09

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 54.84  E-value: 1.09e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334     152 CPDPGVPPGASRRG--NTFDVGYDVTYSCNGNLFLVGSRVRVCQENSQWTGREPAC 205
Cdd:smart00032   1 CPPPPDIENGTVTSssGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
152-205 7.11e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.42  E-value: 7.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777334    152 CPDPGVPPGA--SRRGNTFDVGYDVTYSCNGNLFLVGSRVRVCQENSQWTGREPAC 205
Cdd:pfam00084   1 CPPPPDIPNGkvSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02639 PHA02639
EEV host range protein; Provisional
 30-258 8.99e-08

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 54.28  E-value: 8.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    30 EIQGGTYT-LTKGLETNSLLVYQCPDNFYPYPDTIRVCHPNKQ---WKPRPKkfspqRCKPVECPDPNVLENGNVFPPLE 105
Cdd:PHA02639  27 DISNGFITeLMEKYEIGKLIEYTCNTDYALIGDRFRTCIKDKNnaiWSNKAP-----FCMLKECNDPPSIINGKIYNKRE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334   106 RYLAGNTTTFEC--YSG--YTMRGSSSRTCLSNGKWSGSTTICSRDSgdaCPDPGVPPG---ASRRGNTFDVGYDVTYSC 178
Cdd:PHA02639 102 MYKVGDEIYYVCneHKGvqYSLVGNEKITCIQDKSWKPDPPICKMIN---CRFPALQNGyinGIPSNKKFYYKTRVGFSC 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334   179 NGNLFLVGSRVRVCQENSQWTGREPACYSKFTYDTS---QEVSEAFGS-SIKDSLTTLQPTNDTQAGRKIRISKNGTLNI 254
Cdd:PHA02639 179 KSGFDLVGEKYSTCNINATWFPSIPTCVRNKPIDDIiylKPVDDNFDDlDNEDKINTILHNNDANSTRINQEKENGNIFT 258


                 ....
gi 1777334   255 YIAL 258
Cdd:PHA02639 259 VIIL 262
PHA02831 PHA02831
EEV host range protein; Provisional
 40-215 2.73e-07

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 52.69  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    40 KGLETNSLLVYQCPDNFypypDTIRVCHPNKQWKPRPKKFSPQRCKpvecpDPNVLENGNVFPPLERYLAGNTTTFEC-- 117
Cdd:PHA02831  38 KVYEENENLEYKCNNNF----DKVFVTCNNGSWSTKNMCIGKRNCK-----DPVTILNGYIKNKKDQYSFGDSVTYACkv 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334   118 --YSGYTMRGSSSRTCLsNGKWSGSTTICSRDSgdaCPDPGVPPG-ASRRGNTFDVGYDVTYSCNGNLFLVGSRVRVCQE 194
Cdd:PHA02831 109 nkLEKYSIVGNETVKCI-NKQWVPKYPVCKLIR---CKYPALQNGfLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDI 184

                        170       180
                 ....*....|....*....|.
gi 1777334   195 NSQWTGREPACYSKFTYDTSQ 215
Cdd:PHA02831 185 NSIWYPGIPKCVKDKVHNEIQ 205
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 227-452 5.15e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 51.86  E-value: 5.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  227 DSLTTLQPTNDTQAGRKIRISKNGTLNIYIALDISESVEEEH-FKRAKLAIITLIKKIAAFTvspNYEILFFSADVYEVV 305
Cdd:COG1240  68 LLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLL 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  306 SIVEfyegkiTLESAIKNLEDFQIGDkstGTDVNAALkkfEEGMAWIEQKTGDKfseHRHVFLLfTDGAYNMGGSPLPTL 385
Cdd:COG1240 145 PLTR------DREALKRALDELPPGG---GTPLGDAL---ALALELLKRADPAR---RKVIVLL-TDGRDNAGRIDPLEA 208

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1777334  386 AR-IKNRvymsptgdpGSRLdylesYVFGIGANIFDDDLLP-LTAGTEGElhYFRLKKETNLAATFDDI 452
Cdd:COG1240 209 AElAAAA---------GIRI-----YTIGVGTEAVDEGLLReIAEATGGR--YFRADDLSELAAIYREI 261
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 83-205 1.18e-06

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 50.81  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    83 RCKPVECPDPNVLENGNVfpPLERYLAGNTTTFECYSGYTMRGSSSRTCL--SNGK--WSGSTTICSRDSgdaCPDPgvP 158
Cdd:PHA02927  80 QCIKRRCPSPRDIDNGQL--DIGGVDFGSSITYSCNSGYQLIGESKSYCElgSTGSmvWNPEAPICESVK---CQSP--P 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1777334   159 PGASRRGNTFDVGYD----VTYSCNGNLFLVGSRVRVCQeNSQWTGrEPAC 205
Cdd:PHA02927 153 SISNGRHNGYEDFYTdgsvVTYSCNSGYSLIGNSGVLCS-GGEWSD-PPTC 201
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 250-373 3.75e-06

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 48.15  E-value: 3.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  250 GTLNIYIALDISESVEEEHFKRAKLAIITLIKKIAAFTVSP------NYEILFFSADVYEVVSIVEFYEGKITLESAIKN 323
Cdd:cd01480   1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKdpagswRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAVDN 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 1777334  324 LEdfQIGDkstGTDVNAALKkfeegmawieqKTGDKFSEHRH-----VFLLFTDG 373
Cdd:cd01480  81 LE--YIGG---GTFTDCALK-----------YATEQLLEGSHqkenkFLLVITDG 119
PHA02639 PHA02639
EEV host range protein; Provisional
 85-205 4.34e-06

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 49.28  E-value: 4.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    85 KPVECPDPNVLENGNVFPPLERYLAGNTTTFECYSGYTMRGSSSRTCL---SNGKWSGSTTICSRDSgdaCPDPG--VPP 159
Cdd:PHA02639  18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIkdkNNAIWSNKAPFCMLKE---CNDPPsiING 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 1777334   160 GASRRGNTFDVGYDVTYSCNGN----LFLVGSRVRVCQENSQWTGREPAC 205
Cdd:PHA02639  95 KIYNKREMYKVGDEIYYVCNEHkgvqYSLVGNEKITCIQDKSWKPDPPIC 144
PHA02817 PHA02817
EEV Host range protein; Provisional
 84-205 1.29e-05

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 47.24  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    84 CKPVECPDPNVLENGNVFPPLERYLAGNTTTFECYSG-----YTMRGSSSRTCLSNGKWSGSTTICSRDsgdACPDPGVP 158
Cdd:PHA02817  19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKII---RCRFPALQ 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 1777334   159 PGASR---RGNTFDVGYDVTYSCNGNLFLVGSRVRVCQENSQWTGREPAC 205
Cdd:PHA02817  96 NGFVNgipDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 484-715 1.84e-05

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 46.21  E-value: 1.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  484 VVFINIQGKSPKkCLGSLVSSEFVLTAAHCfIFSDE----PQDVKVEID-DGKGSKEKKVKTFKLHPQYNVTARvkqgva 558
Cdd:COG3591   2 VGRLETDGGGGV-CTGTLIGPNLVLTAGHC-VYDGAgggwATNIVFVPGyNGGPYGTATATRFRVPPGWVASGD------ 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334  559 efYDYDIALIQLERPVQlsisarpicipctketsdalrlpgsatcrdqeelllkNQRERLSFLTRTEPLVGEKdVYAkLG 638
Cdd:COG3591  74 --AGYDYALLRLDEPLG-------------------------------------DTTGWLGLAFNDAPLAGEP-VTI-IG 112

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777334  639 DNRDLCIKKALKAKGITTTdpkvpVTDNFLCTGGDrdhiACTGDSGGAVFKNYESRTIQIALVSWGTQEiCTGGGMR 715
Cdd:COG3591 113 YPGDRPKDLSLDCSGRVTG-----VQGNRLSYDCD----TTGGSSGSPVLDDSDGGGRVVGVHSAGGAD-RANTGVR 179
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 46-146 2.49e-05

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 46.57  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    46 SLLVYQCPDNFYPYPDTIRVChPNKQWKprpkkfSPQRCKPVECPDPNVLeNGNVFPPLER-YLAGNTTTFECYSGYTMR 124
Cdd:PHA02927 170 SVVTYSCNSGYSLIGNSGVLC-SGGEWS------DPPTCQIVKCPHPTIS-NGYLSSGFKRsYSYNDNVDFKCKYGYKLS 241

                         90       100
                 ....*....|....*....|..
gi 1777334   125 GSSSRTCLSNGKWSGSTTICSR 146
Cdd:PHA02927 242 GSSSSTCSPGNTWQPELPKCVR 263
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 84-205 3.25e-04

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 43.54  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777334    84 CKPVECpDPNVLENGNVFPPLERYLAGNTTTFECYSGYTMRGSSSRTCLSNgKWSGSTTiCSRDsgdaCPDPGVPPGASr 163
Cdd:PHA02954 125 CPNAEC-QPLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTAN-SWNVIPS-CQQK----CDIPSLSNGLI- 196

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 1777334   164 RGNTFDVGYDVTYSCNGNLFLVGSRVRVCQEnSQWTGREPAC 205
Cdd:PHA02954 197 SGSTFSIGGVIHLSCKSGFTLTGSPSSTCID-GKWNPVLPIC 237
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH