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Conserved domains on  [gi|974105508|ref|XP_015251708|]
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PREDICTED: complement factor B-like [Cyprinodon variegatus]

Protein Classification

VWA domain-containing protein( domain architecture ID 13332055)

VWA (von Willebrand factor type A) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 255-453 1.79e-84

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.


The actual alignment was detected with superfamily member cd01470:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 198  Bit Score: 266.08  E-value: 1.79e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 255 LNIYIAVDISESIKEEEFDEARNAVITLIRKISSFSVSPNYDIVFFSSEVYRVVNILDFLDGKIklNSVIENLKNFKVGN 334
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDA--DDVIKRLEDFNYDD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 335 K--NTGTDLNLVFKAFEGQMGFIKERvGKERFKDHRHVLIFFTDGAYNMGGSPQPTVARIKNMVYMNQLGEaGSREEYLD 412
Cdd:cd01470   79 HgdKTGTNTAAALKKVYERMALEKVR-NKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSD-NPREDYLD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 974105508 413 IYVFAIGADIFDEDLQPLTTGTGGE-HYFRMKKIVELQETFD 453
Cdd:cd01470  157 VYVFGVGDDVNKEELNDLASKKDNErHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 480-709 5.77e-39

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: 144.34  E-value: 5.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 480 KRRKYPWLVFvINQGIKRKTCIGSLVSPDFVLTAAHCFTfGDEAEHIKI-------DIEDGGKREKKVKKIILHENYNlt 552
Cdd:cd00190    8 KIGSFPWQVS-LQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVrlgshdlSSNEGGGQVIKVKKVIVHPNYN-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 553 akvnegvDEFYDYDVALLRLEEPVRISDVARPICIPCTQEtsdalNLVGESTC------KQQEEVLLKNHRERLSFltrr 626
Cdd:cd00190   84 -------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGY-----NLPAGTTCtvsgwgRTSEGGPLPDVLQEVNV---- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 627 ePLVaekdvfaklgeNRDLCIKKAllaqgittkDERVAVTDNFLCTGGLVEHRDhiACTGDSGGAVFKNHEQRTVQIGVV 706
Cdd:cd00190  148 -PIV-----------SNAECKRAY---------SYGGTITDNMLCAGGLEGGKD--ACQGDSGGPLVCNDNGRGVLVGIV 204


                 ...
gi 974105508 707 SWG 709
Cdd:cd00190  205 SWG 207
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 92-147 8.57e-18

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: 77.89  E-value: 8.57e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508  92 CPDPNVLENGNVFPGQEKYYVGDVTSYDCYSGYTMRGSPSRVCLPNGKWNGSTPIC 147
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 32-208 3.85e-14

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 73.15  E-value: 3.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  32 LDIEGGEYtlsknllpGSLLIYQCHDGYYPYPALTRLCQ--PNGS--WRPPPKRflpqrCKRVECPDPNVLENGNvFPGQ 107
Cdd:PHA02927  97 LDIGGVDF--------GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNPEAPI-----CESVKCQSPPSISNGR-HNGY 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 108 EKYYV-GDVTSYDCYSGYTMRGSPSRVClPNGKWNgSTPICSRDSgdaCPDPGVPPG--ASRVGNMFGIDDRVKYSCNGN 184
Cdd:PHA02927 163 EDFYTdGSVVTYSCNSGYSLIGNSGVLC-SGGEWS-DPPTCQIVK---CPHPTISNGylSSGFKRSYSYNDNVDFKCKYG 237

                        170       180
                 ....*....|....*....|....
gi 974105508 185 LFLIGSKERVCQENGQWTGKEPAC 208
Cdd:PHA02927 238 YKLSGSSSSTCSPGNTWQPELPKC 261
 
Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 255-453 1.79e-84

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: 266.08  E-value: 1.79e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 255 LNIYIAVDISESIKEEEFDEARNAVITLIRKISSFSVSPNYDIVFFSSEVYRVVNILDFLDGKIklNSVIENLKNFKVGN 334
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDA--DDVIKRLEDFNYDD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 335 K--NTGTDLNLVFKAFEGQMGFIKERvGKERFKDHRHVLIFFTDGAYNMGGSPQPTVARIKNMVYMNQLGEaGSREEYLD 412
Cdd:cd01470   79 HgdKTGTNTAAALKKVYERMALEKVR-NKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSD-NPREDYLD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 974105508 413 IYVFAIGADIFDEDLQPLTTGTGGE-HYFRMKKIVELQETFD 453
Cdd:cd01470  157 VYVFGVGDDVNKEELNDLASKKDNErHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 480-709 5.77e-39

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: 144.34  E-value: 5.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 480 KRRKYPWLVFvINQGIKRKTCIGSLVSPDFVLTAAHCFTfGDEAEHIKI-------DIEDGGKREKKVKKIILHENYNlt 552
Cdd:cd00190    8 KIGSFPWQVS-LQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVrlgshdlSSNEGGGQVIKVKKVIVHPNYN-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 553 akvnegvDEFYDYDVALLRLEEPVRISDVARPICIPCTQEtsdalNLVGESTC------KQQEEVLLKNHRERLSFltrr 626
Cdd:cd00190   84 -------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGY-----NLPAGTTCtvsgwgRTSEGGPLPDVLQEVNV---- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 627 ePLVaekdvfaklgeNRDLCIKKAllaqgittkDERVAVTDNFLCTGGLVEHRDhiACTGDSGGAVFKNHEQRTVQIGVV 706
Cdd:cd00190  148 -PIV-----------SNAECKRAY---------SYGGTITDNMLCAGGLEGGKD--ACQGDSGGPLVCNDNGRGVLVGIV 204


                 ...
gi 974105508 707 SWG 709
Cdd:cd00190  205 SWG 207
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 475-711 6.52e-37

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: 138.19  E-value: 6.52e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508   475 GDKTDKRRKYPWLVFVINQGiKRKTCIGSLVSPDFVLTAAHCFTfGDEAEHIKI-----DIEDGGKREK-KVKKIILHEN 548
Cdd:smart00020   4 GGSEANIGSFPWQVSLQYGG-GRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVrlgshDLSSGEEGQViKVSKVIIHPN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508   549 YNltakvnegvDEFYDYDVALLRLEEPVRISDVARPICIPCTQEtsdalNLVGESTC------KQQEEVLLKNHRERLSF 622
Cdd:smart00020  82 YN---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNY-----NVPAGTTCtvsgwgRTSEGAGSLPDTLQEVN 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508   623 LtrrePLVaekdvfaklgeNRDLCIKKAllaqgittkDERVAVTDNFLCTGGLVEHRDhiACTGDSGGAVFKNHEqRTVQ 702
Cdd:smart00020 148 V----PIV-----------SNATCRRAY---------SGGGAITDNMLCAGGLEGGKD--ACQGDSGGPLVCNDG-RWVL 200


                   ....*....
gi 974105508   703 IGVVSWGTH 711
Cdd:smart00020 201 VGIVSWGSG 209
Trypsin pfam00089
Trypsin;
484-709 3.26e-27

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 110.22  E-value: 3.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  484 YPWLVFVINQGiKRKTCIGSLVSPDFVLTAAHCFtfgDEAEHIK-------IDIEDGGKREKKVKKIILHENYNltakvn 556
Cdd:pfam00089  12 FPWQVSLQLSS-GKHFCGGSLISENWVLTAAHCV---SGASDVKvvlgahnIVLREGGEQKFDVEKIIVHPNYN------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  557 egvDEFYDYDVALLRLEEPVRISDVARPICIPctqeTSDALNLVGeSTCKQQEevllknhRERLSFLTRREPLvaekdvf 636
Cdd:pfam00089  82 ---PDTLDNDIALLKLESPVTLGDTVRPICLP----DASSDLPVG-TTCTVSG-------WGNTKTLGPSDTL------- 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974105508  637 aklgenrdLCIKKALLAQGITTKDERVAVTDNFLCTGGlvehRDHIACTGDSGGAVFKNHEQrtvQIGVVSWG 709
Cdd:pfam00089 140 --------QEVTVPVVSRETCRSAYGGTVTDTMICAGA----GGKDACQGDSGGPLVCSDGE---LIGIVSWG 197
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 484-730 4.29e-25

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 105.12  E-value: 4.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 484 YPWLVFVI-NQGIKRKTCIGSLVSPDFVLTAAHCFTfGDEAEHIKI-----DIEDGGKREKKVKKIILHENYNltakvne 557
Cdd:COG5640   42 YPWMVALQsSNGPSGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVvigstDLSTSGGTVVKVARIVVHPDYD------- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 558 gvDEFYDYDVALLRLEEPVrisDVARPICIPCTQETSDA---LNLVG----ESTCKQQEEVLLKnhrerLSFltrrePLV 630
Cdd:COG5640  114 --PATPGNDIALLKLATPV---PGVAPAPLATSADAAAPgtpATVAGwgrtSEGPGSQSGTLRK-----ADV-----PVV 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 631 AEKDVFAKLGenrdlcikkallaqgittkdervAVTDNFLCTGGLVEHRDhiACTGDSGGAVFKNHEQRTVQIGVVSWGT 710
Cdd:COG5640  179 SDATCAAYGG-----------------------FDGGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWGG 233

                        250       260
                 ....*....|....*....|
gi 974105508 711 HQVCSSTDGLVESIDDSRDF 730
Cdd:COG5640  234 GPCAAGYPGVYTRVSAYRDW 253
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 256-459 1.36e-24

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: 101.38  E-value: 1.36e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508   256 NIYIAVDISESIKEEEFDEARNAVITLIRKISSFSVSPNYDIVFFSSEVYRVVNILDFLDgKIKLNSVIENLKNFKVGNK 335
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRS-KDALLEALASLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508   336 NTGTDLNLVFKAFEGQMgfikervgKERFKDHRHVLIFFTDGAYNMGGSPQPTVARiknmvymnqlgEAgsREEYLDIYV 415
Cdd:smart00327  80 NLGAALQYALENLFSKS--------AGSRRGAPKVVILITDGESNDGPKDLLKAAK-----------EL--KRSGVKVFV 138

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 974105508   416 FAIGADIFDEDLQPLTTGTGGEHYFrmkkiveLQETFDKIIDES 459
Cdd:smart00327 139 VGVGNDVDEEELKKLASAPGGVYVF-------LPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
256-454 1.03e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 95.80  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  256 NIYIAVDISESIKEEEFDEARNAVITLIRKISSFSVSPNYDIVFFSSEVYRVVNILDFLDgKIKLNSVIENLKNFKVGNK 335
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSS-KEELLSAVDNLRYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  336 NTGTDLNLVFK-AFEGQMGfikERVGkerfkdHRHVLIFFTDGaYNMGGSPQPTVARIKnmvymnqlgEAGsreeyldIY 414
Cdd:pfam00092  80 NTGKALKYALEnLFSSAAG---ARPG------APKVVVLLTDG-RSQDGDPEEVARELK---------SAG-------VT 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 974105508  415 VFAIG-ADIFDEDLQPLTTGTGGEHYFRMKKIVELQETFDK 454
Cdd:pfam00092 134 VFAVGvGNADDEELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 92-147 8.57e-18

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: 77.89  E-value: 8.57e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508  92 CPDPNVLENGNVFPGQEKYYVGDVTSYDCYSGYTMRGSPSRVCLPNGKWNGSTPIC 147
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 92-147 1.20e-16

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: 74.49  E-value: 1.20e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508    92 CPDPNVLENGNVFPGQEKYYVGDVTSYDCYSGYTMRGSPSRVCLPNGKWNGSTPIC 147
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
92-147 2.64e-15

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 70.61  E-value: 2.64e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508   92 CPDPNVLENGNVFPGQEKYYVGDVTSYDCYSGYTMRGSPSRVCLPNGKWNGSTPIC 147
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 32-208 3.85e-14

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 73.15  E-value: 3.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  32 LDIEGGEYtlsknllpGSLLIYQCHDGYYPYPALTRLCQ--PNGS--WRPPPKRflpqrCKRVECPDPNVLENGNvFPGQ 107
Cdd:PHA02927  97 LDIGGVDF--------GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNPEAPI-----CESVKCQSPPSISNGR-HNGY 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 108 EKYYV-GDVTSYDCYSGYTMRGSPSRVClPNGKWNgSTPICSRDSgdaCPDPGVPPG--ASRVGNMFGIDDRVKYSCNGN 184
Cdd:PHA02927 163 EDFYTdGSVVTYSCNSGYSLIGNSGVLC-SGGEWS-DPPTCQIVK---CPHPTISNGylSSGFKRSYSYNDNVDFKCKYG 237

                        170       180
                 ....*....|....*....|....
gi 974105508 185 LFLIGSKERVCQENGQWTGKEPAC 208
Cdd:PHA02927 238 YKLSGSSSSTCSPGNTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 155-208 7.49e-12

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: 60.94  E-value: 7.49e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508 155 CPDPGVPPGASRVGNM--FGIDDRVKYSCNGNLFLIGSKERVCQENGQWTGKEPAC 208
Cdd:cd00033    1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 48-149 1.36e-10

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 62.75  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  48 GSLLIYQCHDGYYPYPALTRLCQpNGSWRPPPKrflpqrCKRVECPDPNVLeNGNVFPG-QEKYYVGDVTSYDCYSGYTM 126
Cdd:PHA02927 169 GSVVTYSCNSGYSLIGNSGVLCS-GGEWSDPPT------CQIVKCPHPTIS-NGYLSSGfKRSYSYNDNVDFKCKYGYKL 240

                         90       100
                 ....*....|....*....|...
gi 974105508 127 RGSPSRVCLPNGKWNGSTPICSR 149
Cdd:PHA02927 241 SGSSSSTCSPGNTWQPELPKCVR 263
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 155-208 1.69e-10

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: 57.15  E-value: 1.69e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508   155 CPDPGVPPGASRVG--NMFGIDDRVKYSCNGNLFLIGSKERVCQENGQWTGKEPAC 208
Cdd:smart00032   1 CPPPPDIENGTVTSssGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 255-455 3.83e-09

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: 58.41  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 255 LNIYIAVDISESIKEEE-FDEARNAVITLIRKIssfsvsPNYD---IVFFSSEVYRVVNILDfldgkiKLNSVIENLKNF 330
Cdd:COG1240   93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY------RPRDrvgLVAFGGEAEVLLPLTR------DREALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 331 KVGNkntGTDLNL-VFKAFEgqmgfikerVGKERFKDHRHVLIFFTDGAYNMGGSPQPTVARiknmvymnQLGEAGsree 409
Cdd:COG1240  161 PPGG---GTPLGDaLALALE---------LLKRADPARRKVIVLLTDGRDNAGRIDPLEAAE--------LAAAAG---- 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 974105508 410 yLDIYVFAIGADIFDED-LQPLTTGTGGEhYFRMKKIVELQETFDKI 455
Cdd:COG1240  217 -IRIYTIGVGTEAVDEGlLREIAEATGGR-YFRADDLSELAAIYREI 261
Sushi pfam00084
Sushi repeat (SCR repeat);
155-208 7.03e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.42  E-value: 7.03e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508  155 CPDPGVPPGASRVGNM--FGIDDRVKYSCNGNLFLIGSKERVCQENGQWTGKEPAC 208
Cdd:pfam00084   1 CPPPPDIPNGKVSATKneYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 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 ...
 255-453 1.79e-84

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: 266.08  E-value: 1.79e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 255 LNIYIAVDISESIKEEEFDEARNAVITLIRKISSFSVSPNYDIVFFSSEVYRVVNILDFLDGKIklNSVIENLKNFKVGN 334
Cdd:cd01470    1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDA--DDVIKRLEDFNYDD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 335 K--NTGTDLNLVFKAFEGQMGFIKERvGKERFKDHRHVLIFFTDGAYNMGGSPQPTVARIKNMVYMNQLGEaGSREEYLD 412
Cdd:cd01470   79 HgdKTGTNTAAALKKVYERMALEKVR-NKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSD-NPREDYLD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 974105508 413 IYVFAIGADIFDEDLQPLTTGTGGE-HYFRMKKIVELQETFD 453
Cdd:cd01470  157 VYVFGVGDDVNKEELNDLASKKDNErHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 480-709 5.77e-39

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: 144.34  E-value: 5.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 480 KRRKYPWLVFvINQGIKRKTCIGSLVSPDFVLTAAHCFTfGDEAEHIKI-------DIEDGGKREKKVKKIILHENYNlt 552
Cdd:cd00190    8 KIGSFPWQVS-LQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVrlgshdlSSNEGGGQVIKVKKVIVHPNYN-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 553 akvnegvDEFYDYDVALLRLEEPVRISDVARPICIPCTQEtsdalNLVGESTC------KQQEEVLLKNHRERLSFltrr 626
Cdd:cd00190   84 -------PSTYDNDIALLKLKRPVTLSDNVRPICLPSSGY-----NLPAGTTCtvsgwgRTSEGGPLPDVLQEVNV---- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 627 ePLVaekdvfaklgeNRDLCIKKAllaqgittkDERVAVTDNFLCTGGLVEHRDhiACTGDSGGAVFKNHEQRTVQIGVV 706
Cdd:cd00190  148 -PIV-----------SNAECKRAY---------SYGGTITDNMLCAGGLEGGKD--ACQGDSGGPLVCNDNGRGVLVGIV 204


                 ...
gi 974105508 707 SWG 709
Cdd:cd00190  205 SWG 207
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 475-711 6.52e-37

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: 138.19  E-value: 6.52e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508   475 GDKTDKRRKYPWLVFVINQGiKRKTCIGSLVSPDFVLTAAHCFTfGDEAEHIKI-----DIEDGGKREK-KVKKIILHEN 548
Cdd:smart00020   4 GGSEANIGSFPWQVSLQYGG-GRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVrlgshDLSSGEEGQViKVSKVIIHPN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508   549 YNltakvnegvDEFYDYDVALLRLEEPVRISDVARPICIPCTQEtsdalNLVGESTC------KQQEEVLLKNHRERLSF 622
Cdd:smart00020  82 YN---------PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNY-----NVPAGTTCtvsgwgRTSEGAGSLPDTLQEVN 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508   623 LtrrePLVaekdvfaklgeNRDLCIKKAllaqgittkDERVAVTDNFLCTGGLVEHRDhiACTGDSGGAVFKNHEqRTVQ 702
Cdd:smart00020 148 V----PIV-----------SNATCRRAY---------SGGGAITDNMLCAGGLEGGKD--ACQGDSGGPLVCNDG-RWVL 200


                   ....*....
gi 974105508   703 IGVVSWGTH 711
Cdd:smart00020 201 VGIVSWGSG 209
Trypsin pfam00089
Trypsin;
484-709 3.26e-27

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 110.22  E-value: 3.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  484 YPWLVFVINQGiKRKTCIGSLVSPDFVLTAAHCFtfgDEAEHIK-------IDIEDGGKREKKVKKIILHENYNltakvn 556
Cdd:pfam00089  12 FPWQVSLQLSS-GKHFCGGSLISENWVLTAAHCV---SGASDVKvvlgahnIVLREGGEQKFDVEKIIVHPNYN------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  557 egvDEFYDYDVALLRLEEPVRISDVARPICIPctqeTSDALNLVGeSTCKQQEevllknhRERLSFLTRREPLvaekdvf 636
Cdd:pfam00089  82 ---PDTLDNDIALLKLESPVTLGDTVRPICLP----DASSDLPVG-TTCTVSG-------WGNTKTLGPSDTL------- 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974105508  637 aklgenrdLCIKKALLAQGITTKDERVAVTDNFLCTGGlvehRDHIACTGDSGGAVFKNHEQrtvQIGVVSWG 709
Cdd:pfam00089 140 --------QEVTVPVVSRETCRSAYGGTVTDTMICAGA----GGKDACQGDSGGPLVCSDGE---LIGIVSWG 197
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 255-440 1.23e-25

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: 103.53  E-value: 1.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 255 LNIYIAVDISESIKEEEFDEARNAVITLIRKISSFSVSPNYDIVFFSSEVYRVVNILDFLDgKIKLNSVIENLKNFKVGN 334
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKS-KDDLLKAVKNLKYLGGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 335 KNTGTDLNLVFKAFegqmgfikeRVGKERFKDHRHVLIFFTDGAYNMGGSPQPTVARIknmvymnqlgeagsREEYLDIY 414
Cdd:cd01450   80 TNTGKALQYALEQL---------FSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKL--------------KDEGIKVF 136

                        170       180
                 ....*....|....*....|....*.
gi 974105508 415 VFAIGaDIFDEDLQPLTTGTGGEHYF 440
Cdd:cd01450  137 VVGVG-PADEEELREIASCPSERHVF 161
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 484-730 4.29e-25

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 105.12  E-value: 4.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 484 YPWLVFVI-NQGIKRKTCIGSLVSPDFVLTAAHCFTfGDEAEHIKI-----DIEDGGKREKKVKKIILHENYNltakvne 557
Cdd:COG5640   42 YPWMVALQsSNGPSGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVvigstDLSTSGGTVVKVARIVVHPDYD------- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 558 gvDEFYDYDVALLRLEEPVrisDVARPICIPCTQETSDA---LNLVG----ESTCKQQEEVLLKnhrerLSFltrrePLV 630
Cdd:COG5640  114 --PATPGNDIALLKLATPV---PGVAPAPLATSADAAAPgtpATVAGwgrtSEGPGSQSGTLRK-----ADV-----PVV 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 631 AEKDVFAKLGenrdlcikkallaqgittkdervAVTDNFLCTGGLVEHRDhiACTGDSGGAVFKNHEQRTVQIGVVSWGT 710
Cdd:COG5640  179 SDATCAAYGG-----------------------FDGGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWGG 233

                        250       260
                 ....*....|....*....|
gi 974105508 711 HQVCSSTDGLVESIDDSRDF 730
Cdd:COG5640  234 GPCAAGYPGVYTRVSAYRDW 253
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 256-459 1.36e-24

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: 101.38  E-value: 1.36e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508   256 NIYIAVDISESIKEEEFDEARNAVITLIRKISSFSVSPNYDIVFFSSEVYRVVNILDFLDgKIKLNSVIENLKNFKVGNK 335
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRS-KDALLEALASLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508   336 NTGTDLNLVFKAFEGQMgfikervgKERFKDHRHVLIFFTDGAYNMGGSPQPTVARiknmvymnqlgEAgsREEYLDIYV 415
Cdd:smart00327  80 NLGAALQYALENLFSKS--------AGSRRGAPKVVILITDGESNDGPKDLLKAAK-----------EL--KRSGVKVFV 138

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 974105508   416 FAIGADIFDEDLQPLTTGTGGEHYFrmkkiveLQETFDKIIDES 459
Cdd:smart00327 139 VGVGNDVDEEELKKLASAPGGVYVF-------LPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
256-454 1.03e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 95.80  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  256 NIYIAVDISESIKEEEFDEARNAVITLIRKISSFSVSPNYDIVFFSSEVYRVVNILDFLDgKIKLNSVIENLKNFKVGNK 335
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSS-KEELLSAVDNLRYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  336 NTGTDLNLVFK-AFEGQMGfikERVGkerfkdHRHVLIFFTDGaYNMGGSPQPTVARIKnmvymnqlgEAGsreeyldIY 414
Cdd:pfam00092  80 NTGKALKYALEnLFSSAAG---ARPG------APKVVVLLTDG-RSQDGDPEEVARELK---------SAG-------VT 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 974105508  415 VFAIG-ADIFDEDLQPLTTGTGGEHYFRMKKIVELQETFDK 454
Cdd:pfam00092 134 VFAVGvGNADDEELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 255-440 2.04e-19

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: 85.70  E-value: 2.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 255 LNIYIAVDISESIKEEEFDEARNAVITLIRKISSFSVSPNYDIVFFSSEVYRVVNILDFLDgKIKLNSVIENLKNFKVGN 334
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTD-KADLLEAIDALKKGLGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 335 KNTGTDLNLVFKAFEgqmgfikervgKERFKDHRHVLIFFTDGAYNmgGSPQPTVARIKNMvymnqlgeagsREEYLDIY 414
Cdd:cd00198   80 TNIGAALRLALELLK-----------SAKRPNARRVIILLTDGEPN--DGPELLAEAAREL-----------RKLGITVY 135

                        170       180
                 ....*....|....*....|....*.
gi 974105508 415 VFAIGADIFDEDLQPLTTGTGGEHYF 440
Cdd:cd00198  136 TIGIGDDANEDELKEIADKTTGGAVF 161
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 92-147 8.57e-18

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: 77.89  E-value: 8.57e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508  92 CPDPNVLENGNVFPGQEKYYVGDVTSYDCYSGYTMRGSPSRVCLPNGKWNGSTPIC 147
Cdd:cd00033    1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 92-147 1.20e-16

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: 74.49  E-value: 1.20e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508    92 CPDPNVLENGNVFPGQEKYYVGDVTSYDCYSGYTMRGSPSRVCLPNGKWNGSTPIC 147
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
92-147 2.64e-15

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 70.61  E-value: 2.64e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508   92 CPDPNVLENGNVFPGQEKYYVGDVTSYDCYSGYTMRGSPSRVCLPNGKWNGSTPIC 147
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 32-208 3.85e-14

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 73.15  E-value: 3.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  32 LDIEGGEYtlsknllpGSLLIYQCHDGYYPYPALTRLCQ--PNGS--WRPPPKRflpqrCKRVECPDPNVLENGNvFPGQ 107
Cdd:PHA02927  97 LDIGGVDF--------GSSITYSCNSGYQLIGESKSYCElgSTGSmvWNPEAPI-----CESVKCQSPPSISNGR-HNGY 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 108 EKYYV-GDVTSYDCYSGYTMRGSPSRVClPNGKWNgSTPICSRDSgdaCPDPGVPPG--ASRVGNMFGIDDRVKYSCNGN 184
Cdd:PHA02927 163 EDFYTdGSVVTYSCNSGYSLIGNSGVLC-SGGEWS-DPPTCQIVK---CPHPTISNGylSSGFKRSYSYNDNVDFKCKYG 237

                        170       180
                 ....*....|....*....|....
gi 974105508 185 LFLIGSKERVCQENGQWTGKEPAC 208
Cdd:PHA02927 238 YKLSGSSSSTCSPGNTWQPELPKC 261
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 155-208 7.49e-12

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: 60.94  E-value: 7.49e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508 155 CPDPGVPPGASRVGNM--FGIDDRVKYSCNGNLFLIGSKERVCQENGQWTGKEPAC 208
Cdd:cd00033    1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 48-149 1.36e-10

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 62.75  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  48 GSLLIYQCHDGYYPYPALTRLCQpNGSWRPPPKrflpqrCKRVECPDPNVLeNGNVFPG-QEKYYVGDVTSYDCYSGYTM 126
Cdd:PHA02927 169 GSVVTYSCNSGYSLIGNSGVLCS-GGEWSDPPT------CQIVKCPHPTIS-NGYLSSGfKRSYSYNDNVDFKCKYGYKL 240

                         90       100
                 ....*....|....*....|...
gi 974105508 127 RGSPSRVCLPNGKWNGSTPICSR 149
Cdd:PHA02927 241 SGSSSSTCSPGNTWQPELPKCVR 263
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 155-208 1.69e-10

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: 57.15  E-value: 1.69e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508   155 CPDPGVPPGASRVG--NMFGIDDRVKYSCNGNLFLIGSKERVCQENGQWTGKEPAC 208
Cdd:smart00032   1 CPPPPDIENGTVTSssGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 255-455 3.83e-09

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: 58.41  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 255 LNIYIAVDISESIKEEE-FDEARNAVITLIRKIssfsvsPNYD---IVFFSSEVYRVVNILDfldgkiKLNSVIENLKNF 330
Cdd:COG1240   93 RDVVLVVDASGSMAAENrLEAAKGALLDFLDDY------RPRDrvgLVAFGGEAEVLLPLTR------DREALKRALDEL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 331 KVGNkntGTDLNL-VFKAFEgqmgfikerVGKERFKDHRHVLIFFTDGAYNMGGSPQPTVARiknmvymnQLGEAGsree 409
Cdd:COG1240  161 PPGG---GTPLGDaLALALE---------LLKRADPARRKVIVLLTDGRDNAGRIDPLEAAE--------LAAAAG---- 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 974105508 410 yLDIYVFAIGADIFDED-LQPLTTGTGGEhYFRMKKIVELQETFDKI 455
Cdd:COG1240  217 -IRIYTIGVGTEAVDEGlLREIAEATGGR-YFRADDLSELAAIYREI 261
PHA02639 PHA02639
EEV host range protein; Provisional
 27-261 1.26e-08

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 56.98  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  27 CTRNDlDIEGGEYT-LSKNLLPGSLLIYQCHDGYYPYPALTRLC---QPNGSWRPPPKRflpqrCKRVECPDPNVLENGN 102
Cdd:PHA02639  22 CDKPD-DISNGFITeLMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWSNKAPF-----CMLKECNDPPSIINGK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 103 VFPGQEKYYVGDVTSYDC--YSG--YTMRGSPSRVCLPNGKWNGSTPICSRDSgdaCPDPGVPPG---ASRVGNMFGIDD 175
Cdd:PHA02639  96 IYNKREMYKVGDEIYYVCneHKGvqYSLVGNEKITCIQDKSWKPDPPICKMIN---CRFPALQNGyinGIPSNKKFYYKT 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 176 RVKYSCNGNLFLIGSKERVCQENGQWTGKEPACYFKHTYDTP---KEVSEEFGSAI-KDTLTTSQSLNDTQEGRKIRISK 251
Cdd:PHA02639 173 RVGFSCKSGFDLVGEKYSTCNINATWFPSIPTCVRNKPIDDIiylKPVDDNFDDLDnEDKINTILHNNDANSTRINQEKE 252

                        250
                 ....*....|
gi 974105508 252 NGtlNIYIAV 261
Cdd:PHA02639 253 NG--NIFTVI 260
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 83-208 2.41e-08

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 55.81  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  83 LPQRCKRVECPDPNVLENGNVFPGQEKYyvGDVTSYDCYSGYTMRGSPSRVCLPNGK----WNGSTPICSRDSgdaCPdp 158
Cdd:PHA02927  77 LFNQCIKRRCPSPRDIDNGQLDIGGVDF--GSSITYSCNSGYQLIGESKSYCELGSTgsmvWNPEAPICESVK---CQ-- 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508 159 gVPPGASRvGNMFGIDD------RVKYSCNGNLFLIGSKERVCQeNGQWTgKEPAC 208
Cdd:PHA02927 150 -SPPSISN-GRHNGYEDfytdgsVVTYSCNSGYSLIGNSGVLCS-GGEWS-DPPTC 201
PHA02817 PHA02817
EEV Host range protein; Provisional
 87-208 4.58e-08

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 54.56  E-value: 4.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  87 CKRVECPDPNVLENGNVFPGQEKYYVGDVTSYDCYSG-----YTMRGSPSRVCLPNGKWNGSTPICSRDsgdACPDPGVP 161
Cdd:PHA02817  19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKII---RCRFPALQ 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 974105508 162 PGASR---VGNMFGIDDRVKYSCNGNLFLIGSKERVCQENGQWTGKEPAC 208
Cdd:PHA02817  96 NGFVNgipDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
PHA02817 PHA02817
EEV Host range protein; Provisional
 68-149 6.71e-08

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 53.79  E-value: 6.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  68 LCQPNGSWRPPPKRflpqrCKRVECPDPnVLENG--NVFPGQEKYYVGDVTSYDCYSGYTMRGSPSRVCLPNGKWNGSTP 145
Cdd:PHA02817  70 ICEKDGKWNKEFPV-----CKIIRCRFP-ALQNGfvNGIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVP 143


                 ....
gi 974105508 146 ICSR 149
Cdd:PHA02817 144 ICSR 147
Sushi pfam00084
Sushi repeat (SCR repeat);
155-208 7.03e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 49.42  E-value: 7.03e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508  155 CPDPGVPPGASRVGNM--FGIDDRVKYSCNGNLFLIGSKERVCQENGQWTGKEPAC 208
Cdd:pfam00084   1 CPPPPDIPNGKVSATKneYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02831 PHA02831
EEV host range protein; Provisional
 51-208 2.66e-07

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 52.69  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  51 LIYQCHDGYypyPALTRLCQpNGSWRPPpkrflpQRC-KRVECPDPNVLENGNVFPGQEKYYVGDVTSYDC----YSGYT 125
Cdd:PHA02831  46 LEYKCNNNF---DKVFVTCN-NGSWSTK------NMCiGKRNCKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYS 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 126 MRGSPSRVCLpNGKWNGSTPICSRDSgdaCPDPGVPPGASRV-GNMFGIDDRVKYSCNGNLFLIGSKERVCQENGQWTGK 204
Cdd:PHA02831 116 IVGNETVKCI-NKQWVPKYPVCKLIR---CKYPALQNGFLNVfEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPG 191


                 ....
gi 974105508 205 EPAC 208
Cdd:PHA02831 192 IPKC 195
PHA02639 PHA02639
EEV host range protein; Provisional
 88-208 3.53e-07

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 52.74  E-value: 3.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  88 KRVECPDPNVLENGNVFPGQEKYYVGDVTSYDCYSGYTMRGSPSRVCLP---NGKWNGSTPICSRDSgdaCPDPG--VPP 162
Cdd:PHA02639  18 KSIYCDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIKdknNAIWSNKAPFCMLKE---CNDPPsiING 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 974105508 163 GASRVGNMFGIDDRVKYSCNGN----LFLIGSKERVCQENGQWTGKEPAC 208
Cdd:PHA02639  95 KIYNKREMYKVGDEIYYVCNEHkgvqYSLVGNEKITCIQDKSWKPDPPIC 144
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 491-576 1.21e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 49.67  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 491 INQGIKRKTCIGSLVSPDFVLTAAHC-FTFGDEAEHIKIDIEDGGKREK----KVKKIILHENYNLTAKVNegvdefydY 565
Cdd:COG3591    5 LETDGGGGVCTGTLIGPNLVLTAGHCvYDGAGGGWATNIVFVPGYNGGPygtaTATRFRVPPGWVASGDAG--------Y 76

                         90
                 ....*....|.
gi 974105508 566 DVALLRLEEPV 576
Cdd:COG3591   77 DYALLRLDEPL 87
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 87-208 8.69e-06

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 48.54  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  87 CKRVECpDPNVLENGNVFPGQEKYYVGDVTSYDCYSGYTMRGSPSRVCLPNgKWNgSTPICSRDsgdaCPDPGVPPGASR 166
Cdd:PHA02954 125 CPNAEC-QPLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTAN-SWN-VIPSCQQK----CDIPSLSNGLIS 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 974105508 167 vGNMFGIDDRVKYSCNGNLFLIGSKERVCQEnGQWTGKEPAC 208
Cdd:PHA02954 198 -GSTFSIGGVIHLSCKSGFTLTGSPSSTCID-GKWNPVLPIC 237
PHA02831 PHA02831
EEV host range protein; Provisional
 80-151 1.06e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 47.68  E-value: 1.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974105508  80 KRFLPQR--CKRVECPDPnVLENG--NVFpgQEKYYVGDVTSYDCYSGYTMRGSPSRVCLPNGKWNGSTPICSRDS 151
Cdd:PHA02831 127 KQWVPKYpvCKLIRCKYP-ALQNGflNVF--EKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGIPKCVKDK 199
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 33-79 2.88e-05

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: 42.13  E-value: 2.88e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 974105508    33 DIEGGEYTLSKNLLP-GSLLIYQCHDGYYPYPALTRLCQPNGSWRPPP 79
Cdd:smart00032   6 DIENGTVTSSSGTYSyGDTVTYSCDPGYTLIGSSTITCLENGTWSPPP 53
Sushi pfam00084
Sushi repeat (SCR repeat);
33-79 2.94e-05

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 42.10  E-value: 2.94e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 974105508   33 DIEGGEYTLSKN-LLPGSLLIYQCHDGYYPYPALTRLCQPNGSWRPPP 79
Cdd:pfam00084   6 DIPNGKVSATKNeYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPF 53
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 48-156 4.02e-05

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 46.23  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508  48 GSLLIYQCHDGYYPYPALTRLCQPNgSWRPPPKrflpqrCKRvECPDPNvLENGNVfpGQEKYYVGDVTSYDCYSGYTMR 127
Cdd:PHA02954 150 GEHITINCDVGYEVIGASYISCTAN-SWNVIPS------CQQ-KCDIPS-LSNGLI--SGSTFSIGGVIHLSCKSGFTLT 218

                         90       100
                 ....*....|....*....|....*....
gi 974105508 128 GSPSRVCLpNGKWNGSTPICSRDSGDACP 156
Cdd:PHA02954 219 GSPSSTCI-DGKWNPVLPICVRSNEEFDP 246
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 33-79 5.35e-05

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: 41.29  E-value: 5.35e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 974105508  33 DIEGGEYTLSK-NLLPGSLLIYQCHDGYYPYPALTRLCQPNGSWRPPP 79
Cdd:cd00033    6 VPENGTVTGSKgSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPP 53
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 253-377 9.78e-05

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: 43.91  E-value: 9.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 253 GTLNIYIAVDISESIKEEEFDEARNAVITLIRKISSFSVSP------NYDIVFFSSEVYRVVNILDFLDGKIKLNSVIEN 326
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKdpagswRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAVDN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 974105508 327 LKNFkvgnkNTGTDLNlvfKAfegqMGFIKERVGKERFKDHRHVLIFFTDG 377
Cdd:cd01480   81 LEYI-----GGGTFTD---CA----LKYATEQLLEGSHQKENKFLLVITDG 119
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 256-441 1.19e-03

VWA BatA type: 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. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 40.39  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 256 NIYIAVDISESIKEEEFD-EAR-NAVITLIRKISSFSVSPNYDIVFFSSEVYRVVNI-LDfldgKIKLNSVIENLKNFKV 332
Cdd:cd01467    4 DIMIALDVSGSMLAQDFVkPSRlEAAKEVLSDFIDRRENDRIGLVVFAGAAFTQAPLtLD----RESLKELLEDIKIGLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 333 GNKNT-GTDLNLVFKAFegqmgfiKERVGKERfkdhrhVLIFFTDGAYNMGGSPQPTVARI-KNM---VYMNQLGEAGSR 407
Cdd:cd01467   80 GQGTAiGDAIGLAIKRL-------KNSEAKER------VIVLLTDGENNAGEIDPATAAELaKNKgvrIYTIGVGKSGSG 146

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 974105508 408 EEYldiyvfaIGADIFDED-LQPLTTGTGGEHYFR 441
Cdd:cd01467  147 PKP-------DGSTILDEDsLVEIADKTGGRIFRA 174
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 256-377 5.23e-03

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 38.36  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974105508 256 NIYIAVDISESIKEEEFDEARNAVITLirkISSFSVSPN---YDIVFFSSEVyRVVNILDFLDGKiklNSVIENLKNFKV 332
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKDFVKRV---VERLDIGPDgvrVGVVQYSDDP-RTEFYLNTYRSK---DDVLEAVKNLRY 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 974105508 333 GNKNTGTDLNLVF---KAFEGQMGfIKERVGKerfkdhrhVLIFFTDG 377
Cdd:cd01472   75 IGGGTNTGKALKYvreNLFTEASG-SREGVPK--------VLVVITDG 113
 
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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