|
Name |
Accession |
Description |
Interval |
E-value |
| vWA_complement_factors |
cd01470 |
Complement factors B and C2 are two critical proteases for complement activation. They both ... |
10-207 |
1.74e-96 |
|
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: 290.34 E-value: 1.74e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 10 LNLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHE 89
Cdd:cd01470 1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 90 NGTGTNTYAALNSVYLMmnnqMRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RNDYLD 164
Cdd:cd01470 81 DKTGTNTAAALKKVYER----MALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpREDYLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
2ODP_A 165 IYAIGVGKlDVDWRELNELGSKKDGERHAFILQDTKALHQVFE 207
Cdd:cd01470 157 VYVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
230-499 |
3.01e-41 |
|
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: 147.81 E-value: 3.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 230 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 304
Cdd:cd00190 7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 305 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 379
Cdd:cd00190 86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 380 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 458
Cdd:cd00190 141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207
|
250 260 270 280
....*....|....*....|....*....|....*....|.
2ODP_A 459 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 499
Cdd:cd00190 208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
230-462 |
2.80e-39 |
|
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: 142.43 E-value: 2.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 230 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSQWGKE---FLIEKAVISPGFDvfa 305
Cdd:smart00020 8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 306 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 381
Cdd:smart00020 84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 382 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRfRFFQVGLVSWGlyN 460
Cdd:smart00020 148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDG-RWVLVGIVSWG--S 208
|
..
2ODP_A 461 PC 462
Cdd:smart00020 209 GC 210
|
|
| VWA |
pfam00092 |
von Willebrand factor type A domain; |
11-208 |
1.31e-31 |
|
von Willebrand factor type A domain;
Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 119.69 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 11 NLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDNsRDMTEVISSLENANYKDH-E 89
Cdd:pfam00092 1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFP-LNDY-SSKEELLSAVDNLRYLGGgT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 90 NGTGTNTYAALNSVYLMMNNQMRllgmetmawqEIRHAIILLTDGKSNMgGSPKTAVDHIREiLNINqkrndyldIYAIG 169
Cdd:pfam00092 79 TNTGKALKYALENLFSSAAGARP----------GAPKVVVLLTDGRSQD-GDPEEVARELKS-AGVT--------VFAVG 138
|
170 180 190
....*....|....*....|....*....|....*....
2ODP_A 170 VGklDVDWRELNELGSKKDgERHAFILQDTKALHQVFEH 208
Cdd:pfam00092 139 VG--NADDEELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
11-204 |
9.39e-27 |
|
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: 106.38 E-value: 9.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 11 NLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVlnDNSRDMTEVISSLENANYKDhen 90
Cdd:smart00327 1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPL--NDSRSKDALLEALASLSYKL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 91 GTGTNTYAALNSVYLMMNNqmrllgmETMAWQE-IRHAIILLTDGKSNMGGSpktavdhiREILNINQKRNDYLDIYAIG 169
Cdd:smart00327 76 GGGTNLGAALQYALENLFS-------KSAGSRRgAPKVVILITDGESNDGPK--------DLLKAAKELKRSGVKVFVVG 140
|
170 180 190
....*....|....*....|....*....|....*
2ODP_A 170 VGKlDVDWRELNELgSKKDGERHAFILQDTKALHQ 204
Cdd:smart00327 141 VGN-DVDEEELKKL-ASAPGGVYVFLPELLDLLID 173
|
|
| Trypsin |
pfam00089 |
Trypsin; |
236-457 |
1.01e-23 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 99.05 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 236 PWHVTIK-PKSQETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDP----KSQWGKEFLIEKAVISPGFDVFAKKNqg 310
Cdd:pfam00089 13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHnivlREGGEQKFDVEKIIVHPNYNPDTLDN-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 311 ilefygdDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTC------RDHEN---ELLNKQSVPahfvalngsk 381
Cdd:pfam00089 88 -------DIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTCtvsgwgNTKTLgpsDTLQEVTVP---------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2ODP_A 382 lninlkmgvewtscaeVVSQEKtmfpNLTDVREVVTDQFLCSGTQeDESPCKGESGGAVFLERRfrfFQVGLVSWG 457
Cdd:pfam00089 146 ----------------VVSRET----CRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCSDG---ELIGIVSWG 197
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
228-466 |
6.92e-21 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 92.02 E-value: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 228 NASDQERtPWHVTIKPKS---QETCRGALISDQWVLTAAHCFRDGNDHSLwRVNVG--DPKSQWGKEFLIEKAVISPGFD 302
Cdd:COG5640 36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGstDLSTSGGTVVKVARIVVHPDYD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 303 VFAkknqgilefYGDDIALLKLAQKVkmsTHARPICLPctmEANLALRRPQ-------GSTCRDHEN--ELLNKQSVPAh 373
Cdd:COG5640 114 PAT---------PGNDIALLKLATPV---PGVAPAPLA---TSADAAAPGTpatvagwGRTSEGPGSqsGTLRKADVPV- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 374 fvalngsklninlkmgVEWTSCAevvsqektmfpnltDVREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVG 452
Cdd:COG5640 178 ----------------VSDATCA--------------AYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVVKDGGGWVLVG 227
|
250
....*....|....
2ODP_A 453 LVSWGlYNPCLGSA 466
Cdd:COG5640 228 VVSWG-GGPCAAGY 240
|
|
| ChlD |
COG1240 |
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
10-207 |
2.22e-12 |
|
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: 67.27 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 10 LNLYLLLDASQSVSENDFL-IFKESASLMVDRIFSfeiNVSVAIITFASEPKVLMSVlndnSRDMTEVISSLENANYkdh 88
Cdd:COG1240 93 RDVVLVVDASGSMAAENRLeAAKGALLDFLDDYRP---RDRVGLVAFGGEAEVLLPL----TRDREALKRALDELPP--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 89 enGTGTNTYAALNSVYLMMNNQMrllgmetmawQEIRHAIILLTDGKSNMG-GSPKTAVDHIREiLNInqkrndylDIYA 167
Cdd:COG1240 163 --GGGTPLGDALALALELLKRAD----------PARRKVIVLLTDGRDNAGrIDPLEAAELAAA-AGI--------RIYT 221
|
170 180 190 200
....*....|....*....|....*....|....*....|
2ODP_A 168 IGVGKLDVDWRELNELGSKKDGErhAFILQDTKALHQVFE 207
Cdd:COG1240 222 IGVGTEAVDEGLLREIAEATGGR--YFRADDLSELAAIYR 259
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| vWA_complement_factors |
cd01470 |
Complement factors B and C2 are two critical proteases for complement activation. They both ... |
10-207 |
1.74e-96 |
|
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: 290.34 E-value: 1.74e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 10 LNLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHE 89
Cdd:cd01470 1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASDPKEIVSIRDFNSNDADDVIKRLEDFNYDDHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 90 NGTGTNTYAALNSVYLMmnnqMRLLGME-TMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQK----RNDYLD 164
Cdd:cd01470 81 DKTGTNTAAALKKVYER----MALEKVRnKEAFNETRHVIILFTDGKSNMGGSPLPTVDKIKNLVYKNNKsdnpREDYLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
2ODP_A 165 IYAIGVGKlDVDWRELNELGSKKDGERHAFILQDTKALHQVFE 207
Cdd:cd01470 157 VYVFGVGD-DVNKEELNDLASKKDNERHFFKLKDYEDLQEVFD 198
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
230-499 |
3.01e-41 |
|
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: 147.81 E-value: 3.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 230 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGD----PKSQWGKEFLIEKAVISPGFDVF 304
Cdd:cd00190 7 AKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGShdlsSNEGGGQVIKVKKVIVHPNYNPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 305 akknqgileFYGDDIALLKLAQKVKMSTHARPICLPCTMEANlalrrPQGSTCR-----DHENEllnkqsvpahfVALNG 379
Cdd:cd00190 86 ---------TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNL-----PAGTTCTvsgwgRTSEG-----------GPLPD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 380 SKLNINLKMgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVGLVSWGl 458
Cdd:cd00190 141 VLQEVNVPI-VSNAECKRAYSY-----------GGTITDNMLCAGGLEgGKDACQGDSGGPLVCNDNGRGVLVGIVSWG- 207
|
250 260 270 280
....*....|....*....|....*....|....*....|.
2ODP_A 459 ynpcLGSADKNSrkraprskvppPRDFHiNLFRMQPWLRQH 499
Cdd:cd00190 208 ----SGCARPNY-----------PGVYT-RVSSYLDWIQKT 232
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
230-462 |
2.80e-39 |
|
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: 142.43 E-value: 2.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 230 SDQERTPWHVTIKPKS-QETCRGALISDQWVLTAAHCFRdGNDHSLWRVNVGDPKSQWGKE---FLIEKAVISPGFDvfa 305
Cdd:smart00020 8 ANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHDLSSGEEgqvIKVSKVIIHPNYN--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 306 kknqgiLEFYGDDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTCRD----HENEllnkqSVPAHFVALNGSK 381
Cdd:smart00020 84 ------PSTYDNDIALLKLKEPVTLSDNVRPICLPSS-----NYNVPAGTTCTVsgwgRTSE-----GAGSLPDTLQEVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 382 LNInlkmgVEWTSCAEVVSQektmfpnltdvREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRfRFFQVGLVSWGlyN 460
Cdd:smart00020 148 VPI-----VSNATCRRAYSG-----------GGAITDNMLCAGGLEgGKDACQGDSGGPLVCNDG-RWVLVGIVSWG--S 208
|
..
2ODP_A 461 PC 462
Cdd:smart00020 209 GC 210
|
|
| vWFA_subfamily_ECM |
cd01450 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
10-194 |
1.02e-33 |
|
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: 125.10 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 10 LNLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDmtEVISSLENANYKDhe 89
Cdd:cd01450 1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKD--DLLKAVKNLKYLG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 90 nGTGTNTYAALNSVYLMMNNqmrllgmETMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIREIlninqkrndYLDIYAIG 169
Cdd:cd01450 77 -GGGTNTGKALQYALEQLFS-------ESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDE---------GIKVFVVG 139
|
170 180
....*....|....*....|....*
2ODP_A 170 VGklDVDWRELNELGSKKdGERHAF 194
Cdd:cd01450 140 VG--PADEEELREIASCP-SERHVF 161
|
|
| VWA |
pfam00092 |
von Willebrand factor type A domain; |
11-208 |
1.31e-31 |
|
von Willebrand factor type A domain;
Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 119.69 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 11 NLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDNsRDMTEVISSLENANYKDH-E 89
Cdd:pfam00092 1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFP-LNDY-SSKEELLSAVDNLRYLGGgT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 90 NGTGTNTYAALNSVYLMMNNQMRllgmetmawqEIRHAIILLTDGKSNMgGSPKTAVDHIREiLNINqkrndyldIYAIG 169
Cdd:pfam00092 79 TNTGKALKYALENLFSSAAGARP----------GAPKVVVLLTDGRSQD-GDPEEVARELKS-AGVT--------VFAVG 138
|
170 180 190
....*....|....*....|....*....|....*....
2ODP_A 170 VGklDVDWRELNELGSKKDgERHAFILQDTKALHQVFEH 208
Cdd:pfam00092 139 VG--NADDEELRKIASEPG-EGHVFTVSDFEALEDLQDQ 174
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
11-204 |
9.39e-27 |
|
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: 106.38 E-value: 9.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 11 NLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVlnDNSRDMTEVISSLENANYKDhen 90
Cdd:smart00327 1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPL--NDSRSKDALLEALASLSYKL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 91 GTGTNTYAALNSVYLMMNNqmrllgmETMAWQE-IRHAIILLTDGKSNMGGSpktavdhiREILNINQKRNDYLDIYAIG 169
Cdd:smart00327 76 GGGTNLGAALQYALENLFS-------KSAGSRRgAPKVVILITDGESNDGPK--------DLLKAAKELKRSGVKVFVVG 140
|
170 180 190
....*....|....*....|....*....|....*
2ODP_A 170 VGKlDVDWRELNELgSKKDGERHAFILQDTKALHQ 204
Cdd:smart00327 141 VGN-DVDEEELKKL-ASAPGGVYVFLPELLDLLID 173
|
|
| Trypsin |
pfam00089 |
Trypsin; |
236-457 |
1.01e-23 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 99.05 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 236 PWHVTIK-PKSQETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDP----KSQWGKEFLIEKAVISPGFDVFAKKNqg 310
Cdd:pfam00089 13 PWQVSLQlSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHnivlREGGEQKFDVEKIIVHPNYNPDTLDN-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 311 ilefygdDIALLKLAQKVKMSTHARPICLPCTmeanlALRRPQGSTC------RDHEN---ELLNKQSVPahfvalngsk 381
Cdd:pfam00089 88 -------DIALLKLESPVTLGDTVRPICLPDA-----SSDLPVGTTCtvsgwgNTKTLgpsDTLQEVTVP---------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2ODP_A 382 lninlkmgvewtscaeVVSQEKtmfpNLTDVREVVTDQFLCSGTQeDESPCKGESGGAVFLERRfrfFQVGLVSWG 457
Cdd:pfam00089 146 ----------------VVSRET----CRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCSDG---ELIGIVSWG 197
|
|
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
228-466 |
6.92e-21 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 92.02 E-value: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 228 NASDQERtPWHVTIKPKS---QETCRGALISDQWVLTAAHCFRDGNDHSLwRVNVG--DPKSQWGKEFLIEKAVISPGFD 302
Cdd:COG5640 36 PATVGEY-PWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGstDLSTSGGTVVKVARIVVHPDYD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 303 VFAkknqgilefYGDDIALLKLAQKVkmsTHARPICLPctmEANLALRRPQ-------GSTCRDHEN--ELLNKQSVPAh 373
Cdd:COG5640 114 PAT---------PGNDIALLKLATPV---PGVAPAPLA---TSADAAAPGTpatvagwGRTSEGPGSqsGTLRKADVPV- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 374 fvalngsklninlkmgVEWTSCAevvsqektmfpnltDVREVVTDQFLCSGTQE-DESPCKGESGGAVFLERRFRFFQVG 452
Cdd:COG5640 178 ----------------VSDATCA--------------AYGGFDGGTMLCAGYPEgGKDACQGDSGGPLVVKDGGGWVLVG 227
|
250
....*....|....
2ODP_A 453 LVSWGlYNPCLGSA 466
Cdd:COG5640 228 VVSWG-GGPCAAGY 240
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
10-191 |
7.32e-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: 83.77 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 10 LNLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSRDmtEVISSLENANYKdhe 89
Cdd:cd00198 1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKA--DLLEAIDALKKG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 90 NGTGTNTYAALNSVYLMMNNQMRLLGmetmawqeiRHAIILLTDGKSNMGGSPKTAVdhIREIlninqkRNDYLDIYAIG 169
Cdd:cd00198 76 LGGGTNIGAALRLALELLKSAKRPNA---------RRVIILLTDGEPNDGPELLAEA--AREL------RKLGITVYTIG 138
|
170 180
....*....|....*....|..
2ODP_A 170 VGkLDVDWRELNELGSKKDGER 191
Cdd:cd00198 139 IG-DDANEDELKEIADKTTGGA 159
|
|
| ChlD |
COG1240 |
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
10-207 |
2.22e-12 |
|
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: 67.27 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 10 LNLYLLLDASQSVSENDFL-IFKESASLMVDRIFSfeiNVSVAIITFASEPKVLMSVlndnSRDMTEVISSLENANYkdh 88
Cdd:COG1240 93 RDVVLVVDASGSMAAENRLeAAKGALLDFLDDYRP---RDRVGLVAFGGEAEVLLPL----TRDREALKRALDELPP--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 89 enGTGTNTYAALNSVYLMMNNQMrllgmetmawQEIRHAIILLTDGKSNMG-GSPKTAVDHIREiLNInqkrndylDIYA 167
Cdd:COG1240 163 --GGGTPLGDALALALELLKRAD----------PARRKVIVLLTDGRDNAGrIDPLEAAELAAA-AGI--------RIYT 221
|
170 180 190 200
....*....|....*....|....*....|....*....|
2ODP_A 168 IGVGKLDVDWRELNELGSKKDGErhAFILQDTKALHQVFE 207
Cdd:COG1240 222 IGVGTEAVDEGLLREIAEATGGR--YFRADDLSELAAIYR 259
|
|
| YfbK |
COG2304 |
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
10-241 |
4.71e-12 |
|
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];
Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 66.66 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 10 LNLYLLLDASQSVSENDFLIFKESASLMVDRIfsfEINVSVAIITFASEPKVLM-SVLNDNSRDMTEVISSLEnAnykdh 88
Cdd:COG2304 92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL---RPGDRVSIVTFAGDARVLLpPTPATDRAKILAAIDRLQ-A----- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 89 enGTGTNTYAALNSVYlmmnNQMRllgmETMAWQEIRHaIILLTDGKSNMGgspKTAVDHIREILNINQKRNdyLDIYAI 168
Cdd:COG2304 163 --GGGTALGAGLELAY----ELAR----KHFIPGRVNR-VILLTDGDANVG---ITDPEELLKLAEEAREEG--ITLTTL 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2ODP_A 169 GVGkldVDWRE--LNELGSKKDGeRHAFIlQDTKALHQVFEhmldvsKLTDTIcGVGNMSANASDQERTPWHVTI 241
Cdd:COG2304 227 GVG---SDYNEdlLERLADAGGG-NYYYI-DDPEEAEKVFV------REFSRI-GYENRALATEDFPLPYGTLKL 289
|
|
| vWA_collagen |
cd01472 |
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ... |
11-198 |
1.39e-08 |
|
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: 54.16 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 11 NLYLLLDASQSVSENDFLIFKESASLMVDRifsFEI---NVSVAIITFASEPKVlMSVLNdNSRDMTEVISSLENANYKd 87
Cdd:cd01472 2 DIVFLVDGSESIGLSNFNLVKDFVKRVVER---LDIgpdGVRVGVVQYSDDPRT-EFYLN-TYRSKDDVLEAVKNLRYI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 88 henGTGTNTYAALNsvYLMMNNQMRLLGMEtmawQEIRHAIILLTDGKSNMGGspktavdhireILNINQKRNDYLDIYA 167
Cdd:cd01472 76 ---GGGTNTGKALK--YVRENLFTEASGSR----EGVPKVLVVITDGKSQDDV-----------EEPAVELKQAGIEVFA 135
|
170 180 190
....*....|....*....|....*....|.
2ODP_A 168 IGVGKLDVDwrELNELGSkKDGERHAFILQD 198
Cdd:cd01472 136 VGVKNADEE--ELKQIAS-DPKELYVFNVAD 163
|
|
| vWA_Matrilin |
cd01475 |
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ... |
8-230 |
1.93e-08 |
|
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.
Pssm-ID: 238752 [Multi-domain] Cd Length: 224 Bit Score: 54.70 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 8 GHLNLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSVLNDNSR-DMTEVISSLENAnyk 86
Cdd:cd01475 1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKaDLKRAVRRMEYL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 87 dhenGTGTNTYAALNsvYLMMNNQMRLLGMETMAwQEIRHAIILLTDGKSNmggspktavDHIREIlnINQKRNDYLDIY 166
Cdd:cd01475 78 ----ETGTMTGLAIQ--YAMNNAFSEAEGARPGS-ERVPRVGIVVTDGRPQ---------DDVSEV--AAKARALGIEMF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
2ODP_A 167 AIGVGKLDVDwrELNELGSKKDGErHAFILQDTKALHQVfehmldVSKLTDTICGVGNMSANAS 230
Cdd:cd01475 140 AVGVGRADEE--ELREIASEPLAD-HVFYVEDFSTIEEL------TKKFQGKICVVPDLCATLS 194
|
|
| vWA_collagen_alphaI-XII-like |
cd01482 |
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ... |
14-198 |
5.53e-08 |
|
Collagen: 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: 238759 [Multi-domain] Cd Length: 164 Bit Score: 52.29 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 14 LLLDASQSVSENDFlifKESASLMVDRIFSFEI---NVSVAIITFASEPKVLMSVLNDNSRDmtEVISSLENANYKdhen 90
Cdd:cd01482 5 FLVDGSWSIGRSNF---NLVRSFLSSVVEAFEIgpdGVQVGLVQYSDDPRTEFDLNAYTSKE--DVLAAIKNLPYK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 91 GTGTNTYAALNsvYLMMNNQMRLLGMEtmawQEIRHAIILLTDGKSNmggspktavDHIREILNInqKRNDYLDIYAIGV 170
Cdd:cd01482 76 GGNTRTGKALT--HVREKNFTPDAGAR----PGVPKVVILITDGKSQ---------DDVELPARV--LRNLGVNVFAVGV 138
|
170 180
....*....|....*....|....*...
2ODP_A 171 GklDVDWRELNELGSKKDgERHAFILQD 198
Cdd:cd01482 139 K--DADESELKMIASKPS-ETHVFNVAD 163
|
|
| vWA_subgroup |
cd01465 |
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
10-195 |
8.33e-08 |
|
VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.
Pssm-ID: 238742 [Multi-domain] Cd Length: 170 Bit Score: 51.89 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 10 LNLYLLLDASQSVSENDFLIFKESASLMVDRIfsfEINVSVAIITFASEPK-VLMSVLNDNSRDMTEVISSLenanykdh 88
Cdd:cd01465 1 LNLVFVIDRSGSMDGPKLPLVKSALKLLVDQL---RPDDRLAIVTYDGAAEtVLPATPVRDKAAILAAIDRL-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 89 ENGTGTNTYAalnsvylmmnnqmrllGMEtMAWQEIRHA--------IILLTDGKSNMGgspktaVDHIREIL-NINQKR 159
Cdd:cd01465 70 TAGGSTAGGA----------------GIQ-LGYQEAQKHfvpggvnrILLATDGDFNVG------ETDPDELArLVAQKR 126
|
170 180 190
....*....|....*....|....*....|....*...
2ODP_A 160 NDYLDIYAIGVGKldvDWRE--LNELGSKKDGeRHAFI 195
Cdd:cd01465 127 ESGITLSTLGFGD---NYNEdlMEAIADAGNG-NTAYI 160
|
|
| VWA_integrin_invertebrates |
cd01476 |
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ... |
10-195 |
6.17e-07 |
|
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.
Pssm-ID: 238753 [Multi-domain] Cd Length: 163 Bit Score: 49.32 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 10 LNLYLLLDASQSVSEndflIFKESASLMVDRIFSFEIN---VSVAIITFASEPKVLMSVLNDNSRDMTEVISSLENANyk 86
Cdd:cd01476 1 LDLLFVLDSSGSVRG----KFEKYKKYIERIVEGLEIGptaTRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 87 dHENGTgTNTYAALN-SVYLMMNNQMRLLGMETMAwqeirhaiILLTDGKSNmgGSPKTAVDHIREILNInqkrndylDI 165
Cdd:cd01476 75 -FIGGT-TATGAAIEvALQQLDPSEGRREGIPKVV--------VVLTDGRSH--DDPEKQARILRAVPNI--------ET 134
|
170 180 190
....*....|....*....|....*....|.
2ODP_A 166 YAIGVG-KLDVDWRELNELGSKkdgERHAFI 195
Cdd:cd01476 135 FAVGTGdPGTVDTEELHSITGN---EDHIFT 162
|
|
| VWA_2 |
pfam13519 |
von Willebrand factor type A domain; |
12-112 |
9.07e-07 |
|
von Willebrand factor type A domain;
Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 47.29 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 12 LYLLLDASQSVSENDFLIFK-ESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDNSRDMTEVISSLEnanykdhEN 90
Cdd:pfam13519 1 LVFVLDTSGSMRNGDYGPTRlEAAKDAVLALLKSLPGDRVGLVTFGDGPEVLIP-LTKDRAKILRALRRLE-------PK 72
|
90 100
....*....|....*....|..
2ODP_A 91 GTGTNTYAALNSVYLMMNNQMR 112
Cdd:pfam13519 73 GGGTNLAAALQLARAALKHRRK 94
|
|
| vWA_integrins_alpha_subunit |
cd01469 |
Integrins are a class of adhesion receptors that link the extracellular matrix to the ... |
15-202 |
3.42e-06 |
|
Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.
Pssm-ID: 238746 [Multi-domain] Cd Length: 177 Bit Score: 47.35 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 15 LLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDnSRDMTEVISSLENAnykdHENGTGT 94
Cdd:cd01469 6 VLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFT-LNE-YRTKEEPLSLVKHI----SQLLGLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 95 NTYAALNSVylmmnnQMRLLGMETMAWQEIRHAIILLTDGKSNmGGSPKTAVdhireilnINQKRNDYLDIYAIGVGKL- 173
Cdd:cd01469 80 NTATAIQYV------VTELFSESNGARKDATKVLVVITDGESH-DDPLLKDV--------IPQAEREGIIRYAIGVGGHf 144
|
170 180 190
....*....|....*....|....*....|.
2ODP_A 174 --DVDWRELNELGSKKDgERHAFILQDTKAL 202
Cdd:cd01469 145 qrENSREELKTIASKPP-EEHFFNVTDFAAL 174
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
249-328 |
5.81e-06 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 46.98 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 249 CRGALISDQWVLTAAHCF---RDGNDHSLWRVNVGDPKSQWGkEFLIEKAVISPGFDVFAKknqgilefYGDDIALLKLA 325
Cdd:COG3591 14 CTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYG-TATATRFRVPPGWVASGD--------AGYDYALLRLD 84
|
...
2ODP_A 326 QKV 328
Cdd:COG3591 85 EPL 87
|
|
| TerY |
COG4245 |
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]; |
9-185 |
7.33e-06 |
|
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
Pssm-ID: 443387 [Multi-domain] Cd Length: 196 Bit Score: 46.84 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 9 HLNLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEI---NVSVAIITFASEPKVLMsvlndnsrDMTEViSSLENANY 85
Cdd:COG4245 5 RLPVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYaleTVEVSVITFDGEAKVLL--------PLTDL-EDFQPPDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 86 kdhENGTGTNTYAALNSV-YLMMNNQMRLLGMETMAWQEIrhaIILLTDGKSNmGGSPKTAvdhIREILNINQKRNDYld 164
Cdd:COG4245 76 ---SASGGTPLGAALELLlDLIERRVQKYTAEGKGDWRPV---VFLITDGEPT-DSDWEAA---LQRLKDGEAAKKAN-- 143
|
170 180
....*....|....*....|.
2ODP_A 165 IYAIGVGKlDVDWRELNELGS 185
Cdd:COG4245 144 IFAIGVGP-DADTEVLKQLTD 163
|
|
| vWA_micronemal_protein |
cd01471 |
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ... |
10-171 |
6.64e-05 |
|
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.
Pssm-ID: 238748 [Multi-domain] Cd Length: 186 Bit Score: 43.91 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 10 LNLYLLLDASQSVSENDFliFKESASLMVDRIFSFEIN---VSVAIITFASEPKVLMSVLNDNSRD---MTEVISSLENA 83
Cdd:cd01471 1 LDLYLLVDGSGSIGYSNW--VTHVVPFLHTFVQNLNISpdeINLYLVTFSTNAKELIRLSSPNSTNkdlALNAIRALLSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 84 NYKdheNGTgTNTYAALNSVyLMMNNQMRllgmetMAWQEIRHAIILLTDGKSNmggSPKTAVDHIREILNINQKrndyl 163
Cdd:cd01471 79 YYP---NGS-TNTTSALLVV-EKHLFDTR------GNRENAPQLVIIMTDGIPD---SKFRTLKEARKLRERGVI----- 139
|
....*...
2ODP_A 164 dIYAIGVG 171
Cdd:cd01471 140 -IAVLGVG 146
|
|
| ViaA |
COG2425 |
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
12-171 |
1.75e-04 |
|
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];
Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 43.52 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 12 LYLLLDASQSVSENDFLIFKESASLMVDRIFSfeiNVSVAIITFASEPKVLMSVLNDNS-RDMTEVISSLENanykdhen 90
Cdd:COG2425 121 VVLCVDTSGSMAGSKEAAAKAAALALLRALRP---NRRFGVILFDTEVVEDLPLTADDGlEDAIEFLSGLFA-------- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 91 GTGTNTYAALNSvylmmnnqmrllGMETMAWQEIRHA-IILLTDGKSnmGGSPKTAVDHIReilninQKRNDYlDIYAIG 169
Cdd:COG2425 190 GGGTDIAPALRA------------ALELLEEPDYRNAdIVLITDGEA--GVSPEELLREVR------AKESGV-RLFTVA 248
|
..
2ODP_A 170 VG 171
Cdd:COG2425 249 IG 250
|
|
| vWA_collagen_alpha_1-VI-type |
cd01480 |
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ... |
8-136 |
2.30e-04 |
|
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: 41.99 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 8 GHLNLYLLLDASQSVSENDFLIFKESASLMVDRIFSFE------INVSVAIITFASEPKVlMSVLNDNSRDMTEVISSLE 81
Cdd:cd01480 1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYyrkdpaGSWRVGVVQYSDQQEV-EAGFLRDIRNYTSLKEAVD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
2ODP_A 82 NANYKdhenGTGTNTYAALNSVYlmmnNQMRllgmETMAWQEIRHAiILLTDGKS 136
Cdd:cd01480 80 NLEYI----GGGTFTDCALKYAT----EQLL----EGSHQKENKFL-LVITDGHS 121
|
|
| vWA_ATR |
cd01474 |
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ... |
8-213 |
8.67e-04 |
|
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.
Pssm-ID: 238751 [Multi-domain] Cd Length: 185 Bit Score: 40.57 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 8 GHLNLYLLLDASQSVSENDFLIFKESASLmVDRIFSFEINVSvaIITFASEPKVLMSVLNDNSR------DMTEVISSLE 81
Cdd:cd01474 3 GHFDLYFVLDKSGSVAANWIEIYDFVEQL-VDRFNSPGLRFS--FITFSTRATKILPLTDDSSAiikgleVLKKVTPSGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A 82 NANYKDHENGtgtntyaalnsvylmmNNQMRllgMETMAWQEIRHAIILLTDGKsNMGGSPKTAVdhiREilnINQKRND 161
Cdd:cd01474 80 TYIHEGLENA----------------NEQIF---NRNGGGRETVSVIIALTDGQ-LLLNGHKYPE---HE---AKLSRKL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
2ODP_A 162 YLDIYAIGVgkLDVDWRELNELGSKKDgerHAFILQDT-KALHQVFEHMLDVS 213
Cdd:cd01474 134 GAIVYCVGV--TDFLKSQLINIADSKE---YVFPVTSGfQALSGIIESVVKKA 181
|
|
| |
