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Conserved domains on  [gi|1308470224|ref|XP_023144260|]
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complement factor B-like isoform X2 [Amphiprion ocellaris]

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 ...
 254-454 5.86e-83

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: 262.22  E-value: 5.86e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 254 LNIYIAVDISASIEEKHFKNARDAVLKLITKISSFSVTPNYEIVFFSSDVYEVVNILDFLDGKASliSVMEKLSTFTIGE 333
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDAD--DVIKRLEDFNYDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 334 K--NAGTDLNTVFKIFLDRMAFIKRRaGEEGFKEHRHVLIFFTDGAYNMGGSPLPTVERIKNMVYMNNTSDqqkQSREEY 411
Cdd:cd01470    79 HgdKTGTNTAAALKKVYERMALEKVR-NKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSD---NPREDY 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1308470224 412 LDIYVFAIGTVIFDDDLHPLTVGKDG-KHYFRMRDIENLQDTFD 454
Cdd:cd01470   155 LDVYVFGVGDDVNKEELNDLASKKDNeRHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 483-706 1.81e-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: 1.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 483 FPWVAFVIVQKNR--CLGSLVTPRFILTAAHCFkFGDTPEHVTVEL-------DDGDGRVKRVKTFMLHPKYNISakvdq 553
Cdd:cd00190    12 FPWQVSLQYTGGRhfCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLgshdlssNEGGGQVIKVKKVIVHPNYNPS----- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 554 gvkeFYDFDVALIQLEEDVKISAEARPICIPCTQETsnalkLVGDSTC------KQQEEHLLKDQierlnfltrkretvg 627
Cdd:cd00190    86 ----TYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCtvsgwgRTSEGGPLPDV--------------- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308470224 628 LKDVHAKLGDNrDECIKHAltakgittkDERVAVTDNFLCTGGLSPQRDhiACTGDSGGAVFKNYELRTIQVALVSWGS 706
Cdd:cd00190   142 LQEVNVPIVSN-AECKRAY---------SYGGTITDNMLCAGGLEGGKD--ACQGDSGGPLVCNDNGRGVLVGIVSWGS 208
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 91-146 1.02e-17

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: 77.50  E-value: 1.02e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224  91 CPDPNVMENGNVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNGKWSGSTPIC 146
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA02927 super family cl33700
secreted complement-binding protein; Provisional
 44-207 6.15e-15

secreted complement-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02927:

Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 75.46  E-value: 6.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  44 LERGSILVYHCPEGYYPYPHLARVCQPNGR----WNPSpkrfSPQrCRLVECPDPNVMENGNVIPPQEKYFVGNETTYDC 119
Cdd:PHA02927  102 VDFGSSITYSCNSGYQLIGESKSYCELGSTgsmvWNPE----API-CESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSC 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 120 YSGYTLRGSTTRQClPNGKWSgSTPICSRdsgDNCPDPGIPAGASRTG--NIFGIDDTVKYTCNGNLFLVGSSERVCQEN 197
Cdd:PHA02927  177 NSGYSLIGNSGVLC-SGGEWS-DPPTCQI---VKCPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251

                         170
                  ....*....|
gi 1308470224 198 GQWTGKEPAC 207
Cdd:PHA02927  252 NTWQPELPKC 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 ...
 254-454 5.86e-83

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: 262.22  E-value: 5.86e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 254 LNIYIAVDISASIEEKHFKNARDAVLKLITKISSFSVTPNYEIVFFSSDVYEVVNILDFLDGKASliSVMEKLSTFTIGE 333
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDAD--DVIKRLEDFNYDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 334 K--NAGTDLNTVFKIFLDRMAFIKRRaGEEGFKEHRHVLIFFTDGAYNMGGSPLPTVERIKNMVYMNNTSDqqkQSREEY 411
Cdd:cd01470    79 HgdKTGTNTAAALKKVYERMALEKVR-NKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSD---NPREDY 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1308470224 412 LDIYVFAIGTVIFDDDLHPLTVGKDG-KHYFRMRDIENLQDTFD 454
Cdd:cd01470   155 LDVYVFGVGDDVNKEELNDLASKKDNeRHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 483-706 1.81e-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: 1.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 483 FPWVAFVIVQKNR--CLGSLVTPRFILTAAHCFkFGDTPEHVTVEL-------DDGDGRVKRVKTFMLHPKYNISakvdq 553
Cdd:cd00190    12 FPWQVSLQYTGGRhfCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLgshdlssNEGGGQVIKVKKVIVHPNYNPS----- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 554 gvkeFYDFDVALIQLEEDVKISAEARPICIPCTQETsnalkLVGDSTC------KQQEEHLLKDQierlnfltrkretvg 627
Cdd:cd00190    86 ----TYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCtvsgwgRTSEGGPLPDV--------------- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308470224 628 LKDVHAKLGDNrDECIKHAltakgittkDERVAVTDNFLCTGGLSPQRDhiACTGDSGGAVFKNYELRTIQVALVSWGS 706
Cdd:cd00190   142 LQEVNVPIVSN-AECKRAY---------SYGGTITDNMLCAGGLEGGKD--ACQGDSGGPLVCNDNGRGVLVGIVSWGS 208
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 483-706 7.65e-35

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: 132.42  E-value: 7.65e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  483 FPWVAFVIVQKNR--CLGSLVTPRFILTAAHCFkFGDTPEHVTVELDD------GDGRVKRVKTFMLHPKYNisakvdqg 554
Cdd:smart00020  13 FPWQVSLQYGGGRhfCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGShdlssgEEGQVIKVSKVIIHPNYN-------- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  555 vKEFYDFDVALIQLEEDVKISAEARPICIPCTQETsnalkLVGDSTCKQQEEHLLKDQIERLNfltrkretVGLKDVHAK 634
Cdd:smart00020  84 -PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYN-----VPAGTTCTVSGWGRTSEGAGSLP--------DTLQEVNVP 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308470224  635 LGDNrDECIKHAltakgittkDERVAVTDNFLCTGGLSPQRDhiACTGDSGGAVFKNYElRTIQVALVSWGS 706
Cdd:smart00020 150 IVSN-ATCRRAY---------SGGGAITDNMLCAGGLEGGKD--ACQGDSGGPLVCNDG-RWVLVGIVSWGS 208
Trypsin pfam00089
Trypsin;
483-705 9.19e-23

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 97.13  E-value: 9.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 483 FPWVAFVIVQKNR--CLGSLVTPRFILTAAHCFK--------FGDTpehvTVELDDGDGRVKRVKTFMLHPKYNISAkvd 552
Cdd:pfam00089  12 FPWQVSLQLSSGKhfCGGSLISENWVLTAAHCVSgasdvkvvLGAH----NIVLREGGEQKFDVEKIIVHPNYNPDT--- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 553 qgvkefYDFDVALIQLEEDVKISAEARPICIPctqeTSNALKLVGDSTCKQQEEHLLKDQIERLnfltrkretvgLKDVH 632
Cdd:pfam00089  85 ------LDNDIALLKLESPVTLGDTVRPICLP----DASSDLPVGTTCTVSGWGNTKTLGPSDT-----------LQEVT 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308470224 633 AKLGDnRDECIKHAltakgittkdeRVAVTDNFLCTGGLSpqRDhiACTGDSGGAVFKNyelRTIQVALVSWG 705
Cdd:pfam00089 144 VPVVS-RETCRSAY-----------GGTVTDTMICAGAGG--KD--ACQGDSGGPLVCS---DGELIGIVSWG 197
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 483-714 2.18e-22

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 97.41  E-value: 2.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 483 FPWVAFVIV----QKNRCLGSLVTPRFILTAAHCFkFGDTPEHVTV-----ELDDGDGRVKRVKTFMLHPKYNISAkvdq 553
Cdd:COG5640    42 YPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVvigstDLSTSGGTVVKVARIVVHPDYDPAT---- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 554 gvkefYDFDVALIQLEEDVKisaEARPICIPCTQETSNA---LKLVG----DSTCKQQEEHLLKdqierlnfltrkretv 626
Cdd:COG5640   117 -----PGNDIALLKLATPVP---GVAPAPLATSADAAAPgtpATVAGwgrtSEGPGSQSGTLRK---------------- 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 627 glkdVHAKLGDNrDECikhaltakgittKDERVAVTDNFLCTGGLSPQRDhiACTGDSGGAVFKNYELRTIQVALVSWGS 706
Cdd:COG5640   173 ----ADVPVVSD-ATC------------AAYGGFDGGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWGG 233


                  ....*...
gi 1308470224 707 KEmCIGGG 714
Cdd:COG5640   234 GP-CAAGY 240
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 255-458 3.08e-22

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: 94.44  E-value: 3.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  255 NIYIAVDISASIEEKHFKNARDAVLKLITKISSFSVTPNYEIVFFSSDVYEVVNILDFLDgKASLISVMEKLSTFTIGEK 334
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRS-KDALLEALASLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  335 NAGTDLNTVFKIFLDRMAfiKRRAGeegfkeHRHVLIFFTDGAYNMGGSPLptVERIKNMvymnntsdqqkqsREEYLDI 414
Cdd:smart00327  80 NLGAALQYALENLFSKSA--GSRRG------APKVVILITDGESNDGPKDL--LKAAKEL-------------KRSGVKV 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1308470224  415 YVFAIGTVIFDDDLHPLTVGKDGKHYFrmrdienLQDTFDEIID 458
Cdd:smart00327 137 FVVGVGNDVDEEELKKLASAPGGVYVF-------LPELLDLLID 173
VWA pfam00092
von Willebrand factor type A domain;
255-455 4.41e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 93.88  E-value: 4.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 255 NIYIAVDISASIEEKHFKNARDAVLKLITKISSFSVTPNYEIVFFSSDVYEVVNILDFLDgKASLISVMEKLSTFTIGEK 334
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSS-KEELLSAVDNLRYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 335 NAGTDLNTVFKIFLDRMAfikrrageEGFKEHRHVLIFFTDGaYNMGGSPLPTVERIKnmvymnntsdqqkqsrEEYLDI 414
Cdd:pfam00092  80 NTGKALKYALENLFSSAA--------GARPGAPKVVVLLTDG-RSQDGDPEEVARELK----------------SAGVTV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1308470224 415 YVFAIGTVIfDDDLHPLTVGKDGKHYFRMRDIENLQDTFDE 455
Cdd:pfam00092 135 FAVGVGNAD-DEELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 91-146 1.02e-17

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: 77.50  E-value: 1.02e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224  91 CPDPNVMENGNVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNGKWSGSTPIC 146
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 91-146 7.19e-17

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: 74.87  E-value: 7.19e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224   91 CPDPNVMENGNVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNGKWSGSTPIC 146
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 44-207 6.15e-15

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 75.46  E-value: 6.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  44 LERGSILVYHCPEGYYPYPHLARVCQPNGR----WNPSpkrfSPQrCRLVECPDPNVMENGNVIPPQEKYFVGNETTYDC 119
Cdd:PHA02927  102 VDFGSSITYSCNSGYQLIGESKSYCELGSTgsmvWNPE----API-CESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSC 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 120 YSGYTLRGSTTRQClPNGKWSgSTPICSRdsgDNCPDPGIPAGASRTG--NIFGIDDTVKYTCNGNLFLVGSSERVCQEN 197
Cdd:PHA02927  177 NSGYSLIGNSGVLC-SGGEWS-DPPTCQI---VKCPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251

                         170
                  ....*....|
gi 1308470224 198 GQWTGKEPAC 207
Cdd:PHA02927  252 NTWQPELPKC 261
Sushi pfam00084
Sushi repeat (SCR repeat);
91-146 1.15e-13

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 65.98  E-value: 1.15e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224  91 CPDPNVMENGNVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNGKWSGSTPIC 146
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 154-207 1.16e-11

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: 60.17  E-value: 1.16e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224 154 CPDPGIPAGASRTG--NIFGIDDTVKYTCNGNLFLVGSSERVCQENGQWTGKEPAC 207
Cdd:cd00033     1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 154-207 1.78e-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: 56.77  E-value: 1.78e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224  154 CPDPGIPAGASRTG--NIFGIDDTVKYTCNGNLFLVGSSERVCQENGQWTGKEPAC 207
Cdd:smart00032   1 CPPPPDIENGTVTSssGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
154-207 5.54e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 55.58  E-value: 5.54e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224 154 CPDPGIP--AGASRTGNIFGIDDTVKYTCNGNLFLVGSSERVCQENGQWTGKEPAC 207
Cdd:pfam00084   1 CPPPPDIpnGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 47-148 5.46e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 57.74  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  47 GSILVYHCPEGYYPYPHLARVCQpNGRWNpspkrfSPQRCRLVECPDPNVMeNGNVIPPQEKYFVGNETT-YDCYSGYTL 125
Cdd:PHA02927  169 GSVVTYSCNSGYSLIGNSGVLCS-GGEWS------DPPTCQIVKCPHPTIS-NGYLSSGFKRSYSYNDNVdFKCKYGYKL 240

                          90       100
                  ....*....|....*....|...
gi 1308470224 126 RGSTTRQCLPNGKWSGSTPICSR 148
Cdd:PHA02927  241 SGSSSSTCSPGNTWQPELPKCVR 263
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 214-456 2.38e-05

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: 46.86  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 214 DTSLEVSEAFGSAIKDSLTTLESVDDTQEGRKIRISKNGTLNIYIAVDISASIEEKH-FKNARDAVLKLITKISSFSvtp 292
Cdd:COG1240    53 LAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRD--- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 293 NYEIVFFSSDVYEVVnilDFLDGKASLISVMEKLSTftigekNAGTDLntvfkifldRMAFIK-RRAGEEGFKEHRHVLI 371
Cdd:COG1240   130 RVGLVAFGGEAEVLL---PLTRDREALKRALDELPP------GGGTPL---------GDALALaLELLKRADPARRKVIV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 372 FFTDGAYNMG-GSPLPTVERIKNMvymnntsdqqkqsreeylDIYVFAIGTVIFDDDLHPL------TVGKdgkhYFRMR 444
Cdd:COG1240   192 LLTDGRDNAGrIDPLEAAELAAAA------------------GIRIYTIGVGTEAVDEGLLreiaeaTGGR----YFRAD 249

                         250
                  ....*....|..
gi 1308470224 445 DIENLQDTFDEI 456
Cdd:COG1240   250 DLSELAAIYREI 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 ...
 254-454 5.86e-83

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: 262.22  E-value: 5.86e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 254 LNIYIAVDISASIEEKHFKNARDAVLKLITKISSFSVTPNYEIVFFSSDVYEVVNILDFLDGKASliSVMEKLSTFTIGE 333
Cdd:cd01470     1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDAD--DVIKRLEDFNYDD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 334 K--NAGTDLNTVFKIFLDRMAFIKRRaGEEGFKEHRHVLIFFTDGAYNMGGSPLPTVERIKNMVYMNNTSDqqkQSREEY 411
Cdd:cd01470    79 HgdKTGTNTAAALKKVYERMALEKVR-NKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKSD---NPREDY 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1308470224 412 LDIYVFAIGTVIFDDDLHPLTVGKDG-KHYFRMRDIENLQDTFD 454
Cdd:cd01470   155 LDVYVFGVGDDVNKEELNDLASKKDNeRHFFKLKDYEDLQEVFD 198
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 483-706 1.81e-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: 1.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 483 FPWVAFVIVQKNR--CLGSLVTPRFILTAAHCFkFGDTPEHVTVEL-------DDGDGRVKRVKTFMLHPKYNISakvdq 553
Cdd:cd00190    12 FPWQVSLQYTGGRhfCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLgshdlssNEGGGQVIKVKKVIVHPNYNPS----- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 554 gvkeFYDFDVALIQLEEDVKISAEARPICIPCTQETsnalkLVGDSTC------KQQEEHLLKDQierlnfltrkretvg 627
Cdd:cd00190    86 ----TYDNDIALLKLKRPVTLSDNVRPICLPSSGYN-----LPAGTTCtvsgwgRTSEGGPLPDV--------------- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1308470224 628 LKDVHAKLGDNrDECIKHAltakgittkDERVAVTDNFLCTGGLSPQRDhiACTGDSGGAVFKNYELRTIQVALVSWGS 706
Cdd:cd00190   142 LQEVNVPIVSN-AECKRAY---------SYGGTITDNMLCAGGLEGGKD--ACQGDSGGPLVCNDNGRGVLVGIVSWGS 208
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 483-706 7.65e-35

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: 132.42  E-value: 7.65e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  483 FPWVAFVIVQKNR--CLGSLVTPRFILTAAHCFkFGDTPEHVTVELDD------GDGRVKRVKTFMLHPKYNisakvdqg 554
Cdd:smart00020  13 FPWQVSLQYGGGRhfCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGShdlssgEEGQVIKVSKVIIHPNYN-------- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  555 vKEFYDFDVALIQLEEDVKISAEARPICIPCTQETsnalkLVGDSTCKQQEEHLLKDQIERLNfltrkretVGLKDVHAK 634
Cdd:smart00020  84 -PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYN-----VPAGTTCTVSGWGRTSEGAGSLP--------DTLQEVNVP 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308470224  635 LGDNrDECIKHAltakgittkDERVAVTDNFLCTGGLSPQRDhiACTGDSGGAVFKNYElRTIQVALVSWGS 706
Cdd:smart00020 150 IVSN-ATCRRAY---------SGGGAITDNMLCAGGLEGGKD--ACQGDSGGPLVCNDG-RWVLVGIVSWGS 208
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 254-441 1.39e-24

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: 100.83  E-value: 1.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 254 LNIYIAVDISASIEEKHFKNARDAVLKLITKISSFSVTPNYEIVFFSSDVYEVVNILDFLDgKASLISVMEKLSTFTIGE 333
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKS-KDDLLKAVKNLKYLGGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 334 KNAGTDLNTVFkifldRMAFIKRRAGEegfkEHRHVLIFFTDGAYNMGGSPLPTVERIknmvymnntsdqqkqsREEYLD 413
Cdd:cd01450    80 TNTGKALQYAL-----EQLFSESNARE----NVPKVIIVLTDGRSDDGGDPKEAAAKL----------------KDEGIK 134

                         170       180
                  ....*....|....*....|....*...
gi 1308470224 414 IYVFAIGTVIfDDDLHPLTVGKDGKHYF 441
Cdd:cd01450   135 VFVVGVGPAD-EEELREIASCPSERHVF 161
Trypsin pfam00089
Trypsin;
483-705 9.19e-23

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 97.13  E-value: 9.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 483 FPWVAFVIVQKNR--CLGSLVTPRFILTAAHCFK--------FGDTpehvTVELDDGDGRVKRVKTFMLHPKYNISAkvd 552
Cdd:pfam00089  12 FPWQVSLQLSSGKhfCGGSLISENWVLTAAHCVSgasdvkvvLGAH----NIVLREGGEQKFDVEKIIVHPNYNPDT--- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 553 qgvkefYDFDVALIQLEEDVKISAEARPICIPctqeTSNALKLVGDSTCKQQEEHLLKDQIERLnfltrkretvgLKDVH 632
Cdd:pfam00089  85 ------LDNDIALLKLESPVTLGDTVRPICLP----DASSDLPVGTTCTVSGWGNTKTLGPSDT-----------LQEVT 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308470224 633 AKLGDnRDECIKHAltakgittkdeRVAVTDNFLCTGGLSpqRDhiACTGDSGGAVFKNyelRTIQVALVSWG 705
Cdd:pfam00089 144 VPVVS-RETCRSAY-----------GGTVTDTMICAGAGG--KD--ACQGDSGGPLVCS---DGELIGIVSWG 197
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 483-714 2.18e-22

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 97.41  E-value: 2.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 483 FPWVAFVIV----QKNRCLGSLVTPRFILTAAHCFkFGDTPEHVTV-----ELDDGDGRVKRVKTFMLHPKYNISAkvdq 553
Cdd:COG5640    42 YPWMVALQSsngpSGQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVvigstDLSTSGGTVVKVARIVVHPDYDPAT---- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 554 gvkefYDFDVALIQLEEDVKisaEARPICIPCTQETSNA---LKLVG----DSTCKQQEEHLLKdqierlnfltrkretv 626
Cdd:COG5640   117 -----PGNDIALLKLATPVP---GVAPAPLATSADAAAPgtpATVAGwgrtSEGPGSQSGTLRK---------------- 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 627 glkdVHAKLGDNrDECikhaltakgittKDERVAVTDNFLCTGGLSPQRDhiACTGDSGGAVFKNYELRTIQVALVSWGS 706
Cdd:COG5640   173 ----ADVPVVSD-ATC------------AAYGGFDGGTMLCAGYPEGGKD--ACQGDSGGPLVVKDGGGWVLVGVVSWGG 233


                  ....*...
gi 1308470224 707 KEmCIGGG 714
Cdd:COG5640   234 GP-CAAGY 240
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 255-458 3.08e-22

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: 94.44  E-value: 3.08e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  255 NIYIAVDISASIEEKHFKNARDAVLKLITKISSFSVTPNYEIVFFSSDVYEVVNILDFLDgKASLISVMEKLSTFTIGEK 334
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRS-KDALLEALASLSYKLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  335 NAGTDLNTVFKIFLDRMAfiKRRAGeegfkeHRHVLIFFTDGAYNMGGSPLptVERIKNMvymnntsdqqkqsREEYLDI 414
Cdd:smart00327  80 NLGAALQYALENLFSKSA--GSRRG------APKVVILITDGESNDGPKDL--LKAAKEL-------------KRSGVKV 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1308470224  415 YVFAIGTVIFDDDLHPLTVGKDGKHYFrmrdienLQDTFDEIID 458
Cdd:smart00327 137 FVVGVGNDVDEEELKKLASAPGGVYVF-------LPELLDLLID 173
VWA pfam00092
von Willebrand factor type A domain;
255-455 4.41e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 93.88  E-value: 4.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 255 NIYIAVDISASIEEKHFKNARDAVLKLITKISSFSVTPNYEIVFFSSDVYEVVNILDFLDgKASLISVMEKLSTFTIGEK 334
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSS-KEELLSAVDNLRYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 335 NAGTDLNTVFKIFLDRMAfikrrageEGFKEHRHVLIFFTDGaYNMGGSPLPTVERIKnmvymnntsdqqkqsrEEYLDI 414
Cdd:pfam00092  80 NTGKALKYALENLFSSAA--------GARPGAPKVVVLLTDG-RSQDGDPEEVARELK----------------SAGVTV 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1308470224 415 YVFAIGTVIfDDDLHPLTVGKDGKHYFRMRDIENLQDTFDE 455
Cdd:pfam00092 135 FAVGVGNAD-DEELRKIASEPGEGHVFTVSDFEALEDLQDQ 174
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 91-146 1.02e-17

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: 77.50  E-value: 1.02e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224  91 CPDPNVMENGNVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNGKWSGSTPIC 146
Cdd:cd00033     1 CPPPPVPENGTVTGSKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 91-146 7.19e-17

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: 74.87  E-value: 7.19e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224   91 CPDPNVMENGNVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNGKWSGSTPIC 146
Cdd:smart00032   1 CPPPPDIENGTVTSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 254-441 3.15e-16

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: 76.84  E-value: 3.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 254 LNIYIAVDISASIEEKHFKNARDAVLKLITKISSFSVTPNYEIVFFSSDVYEVVNILDFLDgKASLISVMEKLSTFTIGe 333
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTD-KADLLEAIDALKKGLGG- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 334 knaGTDLNTVFKIFLDRMAFIKRRAGeegfkehRHVLIFFTDGAYNmgGSPLPTVERIKNMvymnntsdqqkqsREEYLD 413
Cdd:cd00198    79 ---GTNIGAALRLALELLKSAKRPNA-------RRVIILLTDGEPN--DGPELLAEAAREL-------------RKLGIT 133

                         170       180
                  ....*....|....*....|....*...
gi 1308470224 414 IYVFAIGTVIFDDDLHPLTVGKDGKHYF 441
Cdd:cd00198   134 VYTIGIGDDANEDELKEIADKTTGGAVF 161
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 44-207 6.15e-15

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 75.46  E-value: 6.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  44 LERGSILVYHCPEGYYPYPHLARVCQPNGR----WNPSpkrfSPQrCRLVECPDPNVMENGNVIPPQEKYFVGNETTYDC 119
Cdd:PHA02927  102 VDFGSSITYSCNSGYQLIGESKSYCELGSTgsmvWNPE----API-CESVKCQSPPSISNGRHNGYEDFYTDGSVVTYSC 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 120 YSGYTLRGSTTRQClPNGKWSgSTPICSRdsgDNCPDPGIPAGASRTG--NIFGIDDTVKYTCNGNLFLVGSSERVCQEN 197
Cdd:PHA02927  177 NSGYSLIGNSGVLC-SGGEWS-DPPTCQI---VKCPHPTISNGYLSSGfkRSYSYNDNVDFKCKYGYKLSGSSSSTCSPG 251

                         170
                  ....*....|
gi 1308470224 198 GQWTGKEPAC 207
Cdd:PHA02927  252 NTWQPELPKC 261
Sushi pfam00084
Sushi repeat (SCR repeat);
91-146 1.15e-13

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 65.98  E-value: 1.15e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224  91 CPDPNVMENGNVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNGKWSGSTPIC 146
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 154-207 1.16e-11

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: 60.17  E-value: 1.16e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224 154 CPDPGIPAGASRTG--NIFGIDDTVKYTCNGNLFLVGSSERVCQENGQWTGKEPAC 207
Cdd:cd00033     1 CPPPPVPENGTVTGskGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 154-207 1.78e-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: 56.77  E-value: 1.78e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224  154 CPDPGIPAGASRTG--NIFGIDDTVKYTCNGNLFLVGSSERVCQENGQWTGKEPAC 207
Cdd:smart00032   1 CPPPPDIENGTVTSssGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
154-207 5.54e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 55.58  E-value: 5.54e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1308470224 154 CPDPGIP--AGASRTGNIFGIDDTVKYTCNGNLFLVGSSERVCQENGQWTGKEPAC 207
Cdd:pfam00084   1 CPPPPDIpnGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
PHA02639 PHA02639
EEV host range protein; Provisional
 39-207 8.59e-10

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 60.45  E-value: 8.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  39 KLTNKLERGSILVYHCPEGYYPYPHLARVC---QPNGRW-NPSPkrfspqRCRLVECPDPNVMENGNVIPPQEKYFVGNE 114
Cdd:PHA02639   35 ELMEKYEIGKLIEYTCNTDYALIGDRFRTCikdKNNAIWsNKAP------FCMLKECNDPPSIINGKIYNKREMYKVGDE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 115 TTYDC--YSG--YTLRGSTTRQCLPNGKWSGSTPICSRdsgDNCPDPGIPAG---ASRTGNIFGIDDTVKYTCNGNLFLV 187
Cdd:PHA02639  109 IYYVCneHKGvqYSLVGNEKITCIQDKSWKPDPPICKM---INCRFPALQNGyinGIPSNKKFYYKTRVGFSCKSGFDLV 185

                         170       180
                  ....*....|....*....|
gi 1308470224 188 GSSERVCQENGQWTGKEPAC 207
Cdd:PHA02639  186 GEKYSTCNINATWFPSIPTC 205
PHA02927 PHA02927
secreted complement-binding protein; Provisional
 47-148 5.46e-09

secreted complement-binding protein; Provisional


Pssm-ID: 222943 [Multi-domain]  Cd Length: 263  Bit Score: 57.74  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  47 GSILVYHCPEGYYPYPHLARVCQpNGRWNpspkrfSPQRCRLVECPDPNVMeNGNVIPPQEKYFVGNETT-YDCYSGYTL 125
Cdd:PHA02927  169 GSVVTYSCNSGYSLIGNSGVLCS-GGEWS------DPPTCQIVKCPHPTIS-NGYLSSGFKRSYSYNDNVdFKCKYGYKL 240

                          90       100
                  ....*....|....*....|...
gi 1308470224 126 RGSTTRQCLPNGKWSGSTPICSR 148
Cdd:PHA02927  241 SGSSSSTCSPGNTWQPELPKCVR 263
PHA02831 PHA02831
EEV host range protein; Provisional
 91-207 1.14e-08

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 56.92  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  91 CPDPNVMENGNVIPPQEKYFVGNETTYDC----YSGYTLRGSTTRQCLpNGKWSGSTPICSRDsgdNCPDPGIPAGASRT 166
Cdd:PHA02831   78 CKDPVTILNGYIKNKKDQYSFGDSVTYACkvnkLEKYSIVGNETVKCI-NKQWVPKYPVCKLI---RCKYPALQNGFLNV 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1308470224 167 -GNIFGIDDTVKYTCNGNLFLVGSSERVCQENGQWTGKEPAC 207
Cdd:PHA02831  154 fEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGIPKC 195
PHA02817 PHA02817
EEV Host range protein; Provisional
 67-148 2.04e-08

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 55.33  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  67 VCQPNGRWNPSPKRfspqrCRLVECPDPnVMENG--NVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNGKWSGSTP 144
Cdd:PHA02817   70 ICEKDGKWNKEFPV-----CKIIRCRFP-ALQNGfvNGIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVP 143


                  ....
gi 1308470224 145 ICSR 148
Cdd:PHA02817  144 ICSR 147
PHA02639 PHA02639
EEV host range protein; Provisional
 91-207 1.55e-07

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 53.90  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  91 CPDPNVMENGNVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLP---NGKWSGSTPICSRDSgdnCPDPG--IPAGASR 165
Cdd:PHA02639   22 CDKPDDISNGFITELMEKYEIGKLIEYTCNTDYALIGDRFRTCIKdknNAIWSNKAPFCMLKE---CNDPPsiINGKIYN 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1308470224 166 TGNIFGIDDTVKYTCNGN----LFLVGSSERVCQENGQWTGKEPAC 207
Cdd:PHA02639   99 KREMYKVGDEIYYVCNEHkgvqYSLVGNEKITCIQDKSWKPDPPIC 144
PHA02817 PHA02817
EEV Host range protein; Provisional
 86-207 8.67e-07

EEV Host range protein; Provisional


Pssm-ID: 165167 [Multi-domain]  Cd Length: 225  Bit Score: 50.71  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  86 CRLVECPDPNVMENGNVIPPQEKYFVGNETTYDCYSG-----YTLRGSTTRQCLPNGKWSGSTPICSRDSgdnCPDPgip 160
Cdd:PHA02817   19 CDLNKCCYPPSIKNGYIYNKKTEYNIGSNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIR---CRFP--- 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308470224 161 agASRTGNIFGIDDT--------VKYTCNGNLFLVGSSERVCQENGQWTGKEPAC 207
Cdd:PHA02817   93 --ALQNGFVNGIPDSkkfyyeseVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 494-572 1.83e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 49.29  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 494 NRCLGSLVTPRFILTAAHCF---KFGDTPEHVTVE--LDDGDGRVKRVKTFMLHPKYNISAKvdqgvkefYDFDVALIQL 568
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVpgYNGGPYGTATATRFRVPPGWVASGD--------AGYDYALLRL 83


                  ....
gi 1308470224 569 EEDV 572
Cdd:COG3591    84 DEPL 87
PHA02831 PHA02831
EEV host range protein; Provisional
 17-153 1.05e-05

EEV host range protein; Provisional


Pssm-ID: 165176 [Multi-domain]  Cd Length: 268  Bit Score: 47.68  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  17 LCMGEVqcNCTETNMAMAGGDYKLTNKLERGSILVYHCP----EGYYPYPHLARVCqPNGRWNPSpkrfSPQrCRLVECP 92
Cdd:PHA02831   71 MCIGKR--NCKDPVTILNGYIKNKKDQYSFGDSVTYACKvnklEKYSIVGNETVKC-INKQWVPK----YPV-CKLIRCK 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308470224  93 DPnVMENGNVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNGKWSGSTPICSRDSGDN 153
Cdd:PHA02831  143 YP-ALQNGFLNVFEKKFYYGDIVNFKCKKGFILLGSSVSTCDINSIWYPGIPKCVKDKVHN 202
PHA02954 PHA02954
EEV membrane glycoprotein; Provisional
 89-207 1.07e-05

EEV membrane glycoprotein; Provisional


Pssm-ID: 165263 [Multi-domain]  Cd Length: 317  Bit Score: 48.16  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  89 VECPD----PNVMENGNVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNgKWSgSTPICSRdsgdNCPDPGIPAGAS 164
Cdd:PHA02954  123 VTCPNaecqPLQLEHGSCQPVKEKYSFGEHITINCDVGYEVIGASYISCTAN-SWN-VIPSCQQ----KCDIPSLSNGLI 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1308470224 165 rTGNIFGIDDTVKYTCNGNLFLVGSSERVCQEnGQWTGKEPAC 207
Cdd:PHA02954  197 -SGSTFSIGGVIHLSCKSGFTLTGSPSSTCID-GKWNPVLPIC 237
PHA02639 PHA02639
EEV host range protein; Provisional
 68-149 1.61e-05

EEV host range protein; Provisional


Pssm-ID: 165022 [Multi-domain]  Cd Length: 295  Bit Score: 47.35  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224  68 CQPNGRWNPSPKRfspqrCRLVECPDPnVMENG--NVIPPQEKYFVGNETTYDCYSGYTLRGSTTRQCLPNGKWSGSTPI 145
Cdd:PHA02639  131 CIQDKSWKPDPPI-----CKMINCRFP-ALQNGyiNGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPT 204


                  ....
gi 1308470224 146 CSRD 149
Cdd:PHA02639  205 CVRN 208
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 214-456 2.38e-05

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: 46.86  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 214 DTSLEVSEAFGSAIKDSLTTLESVDDTQEGRKIRISKNGTLNIYIAVDISASIEEKH-FKNARDAVLKLITKISSFSvtp 292
Cdd:COG1240    53 LAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRD--- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 293 NYEIVFFSSDVYEVVnilDFLDGKASLISVMEKLSTftigekNAGTDLntvfkifldRMAFIK-RRAGEEGFKEHRHVLI 371
Cdd:COG1240   130 RVGLVAFGGEAEVLL---PLTRDREALKRALDELPP------GGGTPL---------GDALALaLELLKRADPARRKVIV 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 372 FFTDGAYNMG-GSPLPTVERIKNMvymnntsdqqkqsreeylDIYVFAIGTVIFDDDLHPL------TVGKdgkhYFRMR 444
Cdd:COG1240   192 LLTDGRDNAGrIDPLEAAELAAAA------------------GIRIYTIGVGTEAVDEGLLreiaeaTGGR----YFRAD 249

                         250
                  ....*....|..
gi 1308470224 445 DIENLQDTFDEI 456
Cdd:COG1240   250 DLSELAAIYREI 261
Sushi pfam00084
Sushi repeat (SCR repeat);
26-78 2.39e-04

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 39.40  E-value: 2.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1308470224  26 CTETNMAMAGGDYKLTNKLERGSILVYHCPEGYYPYPHLARVCQPNGRWNPSP 78
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPF 53
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 47-78 2.91e-04

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: 39.43  E-value: 2.91e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1308470224   47 GSILVYHCPEGYYPYPHLARVCQPNGRWNPSP 78
Cdd:smart00032  22 GDTVTYSCDPGYTLIGSSTITCLENGTWSPPP 53
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 47-78 5.16e-04

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: 38.60  E-value: 5.16e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1308470224  47 GSILVYHCPEGYYPYPHLARVCQPNGRWNPSP 78
Cdd:cd00033    22 GSTVTYSCNEGYTLVGSSTITCTENGGWSPPP 53
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 252-390 1.82e-03

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: 40.06  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308470224 252 GTLNIYIAVDISASIEEKHFKNARDAVLKLITKISSFSVTP------NYEIVFFSSDVYEVVNILDFLDGKASLISVMEK 325
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRKdpagswRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAVDN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308470224 326 LSTFtigekNAGTDLNTVFKIFLDRMaFIKRRAGEegfkehRHVLIFFTDGayNMGGSPLPTVER 390
Cdd:cd01480    81 LEYI-----GGGTFTDCALKYATEQL-LEGSHQKE------NKFLLVITDG--HSDGSPDGGIEK 131
 
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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