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Conserved domains on  [gi|126031547|pdb|2ODP|A]
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Chain A, Complement C2

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
10-207 1.58e-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  Cd Length: 198  Bit Score: 290.34  E-value: 1.58e-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 2.74e-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  Cd Length: 232  Bit Score: 147.81  E-value: 2.74e-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
 
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 1.58e-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  Cd Length: 198  Bit Score: 290.34  E-value: 1.58e-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 2.74e-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  Cd Length: 232  Bit Score: 147.81  E-value: 2.74e-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 2.55e-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: 2.55e-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 3.08e-37

von Willebrand factor type A domain.


Pssm-ID: 365868  Cd Length: 173  Bit Score: 134.70  E-value: 3.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A         11 NLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDnSRDMTEVISSLENANYKDHEN 90
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLSKLVESLDIGPDGTRVGLVQYSSEVRTEFP-LND-YSSKEELLSAVDNLRYLGGGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A         91 gtgTNTYAALNSVYLMMNNQMRllgmetmaWQEIRHAIILLTDGKSNMGGSPKTAVDHIREilninqkrnDYLDIYAIGV 170
Cdd:pfam00092  79 ---TNTGKALKYALENLFSSSA--------GENAPKVVILLTDGKSNDGGDPKEVARELKS---------AGVTVFAVGV 138
                         170       180       190
                  ....*....|....*....|....*....|....*...
2ODP_A        171 GklDVDWRELNELGSKKDgERHAFILQDTKALHQVFEH 208
Cdd:pfam00092 139 G--NADNEELNKIASEPD-EGHVFTVSDFEALEDLQDQ 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
11-204 8.55e-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: 8.55e-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 4.71e-24

Trypsin.


Pssm-ID: 365866  Cd Length: 219  Bit Score: 99.82  E-value: 4.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A        236 PWHVTIKPKS-QETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDP----KSQWGKEFLIEKAVISPGFDVFAKKNqg 310
Cdd:pfam00089  13 PWQVSLQLSSgKHFCGGSLISENWVLTAAHCVSGASD---VQVVLGEHnivlREGGEQKFDVAKVIVHPNYNPDTLDN-- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A        311 ilefygdDIALLKLAQKVKMSTHARPICLPcTMEANLALRRP---QGSTCRDHEN--ELLNKQSVPahfvalngsklnin 385
Cdd:pfam00089  88 -------DIALLKLESPVTLGDTVRPICLP-DAGADLPVGTTctvSGWGNTKTLGppDTLQEVTVP-------------- 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2ODP_A        386 lkmgvewtscaeVVSQEKtmfpNLTDVREVVTDQFLCSGTQeDESPCKGESGGAVFLERRfrfFQVGLVSWG 457
Cdd:pfam00089 146 ------------VVSRET----CRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCSDG---ELIGIVSWG 197
 
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 1.58e-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  Cd Length: 198  Bit Score: 290.34  E-value: 1.58e-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 2.74e-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  Cd Length: 232  Bit Score: 147.81  E-value: 2.74e-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 2.55e-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: 2.55e-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 3.08e-37

von Willebrand factor type A domain.


Pssm-ID: 365868  Cd Length: 173  Bit Score: 134.70  E-value: 3.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A         11 NLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDnSRDMTEVISSLENANYKDHEN 90
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLSKLVESLDIGPDGTRVGLVQYSSEVRTEFP-LND-YSSKEELLSAVDNLRYLGGGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A         91 gtgTNTYAALNSVYLMMNNQMRllgmetmaWQEIRHAIILLTDGKSNMGGSPKTAVDHIREilninqkrnDYLDIYAIGV 170
Cdd:pfam00092  79 ---TNTGKALKYALENLFSSSA--------GENAPKVVILLTDGKSNDGGDPKEVARELKS---------AGVTVFAVGV 138
                         170       180       190
                  ....*....|....*....|....*....|....*...
2ODP_A        171 GklDVDWRELNELGSKKDgERHAFILQDTKALHQVFEH 208
Cdd:pfam00092 139 G--NADNEELNKIASEPD-EGHVFTVSDFEALEDLQDQ 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
10-194 9.25e-34

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: 9.25e-34
                        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 smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
11-204 8.55e-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: 8.55e-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 4.71e-24

Trypsin.


Pssm-ID: 365866  Cd Length: 219  Bit Score: 99.82  E-value: 4.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A        236 PWHVTIKPKS-QETCRGALISDQWVLTAAHCFRDGNDhslWRVNVGDP----KSQWGKEFLIEKAVISPGFDVFAKKNqg 310
Cdd:pfam00089  13 PWQVSLQLSSgKHFCGGSLISENWVLTAAHCVSGASD---VQVVLGEHnivlREGGEQKFDVAKVIVHPNYNPDTLDN-- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A        311 ilefygdDIALLKLAQKVKMSTHARPICLPcTMEANLALRRP---QGSTCRDHEN--ELLNKQSVPahfvalngsklnin 385
Cdd:pfam00089  88 -------DIALLKLESPVTLGDTVRPICLP-DAGADLPVGTTctvSGWGNTKTLGppDTLQEVTVP-------------- 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2ODP_A        386 lkmgvewtscaeVVSQEKtmfpNLTDVREVVTDQFLCSGTQeDESPCKGESGGAVFLERRfrfFQVGLVSWG 457
Cdd:pfam00089 146 ------------VVSRET----CRSAYGGTVTDTMICAGAG-GKDACQGDSGGPLVCSDG---ELIGIVSWG 197
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
10-191 6.66e-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: 6.66e-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
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
11-198 1.26e-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: 1.26e-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 1.75e-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: 1.75e-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_2 pfam13519
von Willebrand factor type A domain.
12-135 2.56e-08

von Willebrand factor type A domain.


Pssm-ID: 379234  Cd Length: 107  Bit Score: 51.90  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ODP_A         12 LYLLLDASQSVSENDFLIFK-ESASLMVDRIFSFEINVSVAIITFASEPKVLMSvLNDNSRDMTEVISSLEnanykdhEN 90
Cdd:pfam13519   1 LVFVVDNSGSMRNGDYGPTRlEAAKDAVLALLASLPGDRVGLVTFGDGPEVLIP-LTKDRAKILRALRRLE-------PT 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
2ODP_A         91 GTGTNTYAALNSVYLMMNNQmrllgmetmaWQEIRHAIILLTDGK 135
Cdd:pfam13519  73 GGGTDLAAALQLARAALKHR----------RKNQPRVIVLITDGE 107
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
14-198 5.04e-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  Cd Length: 164  Bit Score: 52.29  E-value: 5.04e-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 7.59e-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: 7.59e-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 5.62e-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: 5.62e-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_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
15-202 3.11e-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  Cd Length: 177  Bit Score: 47.35  E-value: 3.11e-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
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
10-171 6.04e-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: 6.04e-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
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
8-136 2.09e-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  Cd Length: 186  Bit Score: 41.99  E-value: 2.09e-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 7.90e-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  Cd Length: 185  Bit Score: 40.57  E-value: 7.90e-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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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