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Conserved domains on  [gi|392928328|ref|NP_510791|]
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VWFA domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 481-633 5.83e-10

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


The actual alignment was detected with superfamily member cd01450:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 161  Bit Score: 58.84  E-value: 5.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328 481 TDVTILMDNNNDVGSAmEFQNQCRTIAKLIKTWPISPKLMEGEAIVYSTTdggQIVENPF-SYQSASAFANEVMAFDDYY 559
Cdd:cd01450    1 LDIVFLLDGSESVGPE-NFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDD---VRVEFSLnDYKSKDDLLKAVKNLKYLG 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392928328 560 FAASppSLTASLQYVSQNL---GRRRQSRQQATIVFT--YSSSYSDVQTAIEYVTQIGGNLIIVAVGGADQTVLKQLTG 633
Cdd:cd01450   77 GGGT--NTGKALQYALEQLfseSNARENVPKVIIVLTdgRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIAS 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 285-454 1.06e-08

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: 55.54  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328   285 DVIILLDNSNAMkSFTNFNLVKSwIVKTLLPLWLIDREDVQVAFATYaANDFNTLLDF-DEASEEEVASVISAQMYSGKH 363
Cdd:smart00327   1 DVVFLLDGSGSM-GGNRFELAKE-FVLKLVEQLDIGPDGDRVGLVTF-SDDARVLFPLnDSRSKDALLEALASLSYKLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328   364 NSSITYGIRAAGDI------HGLRPVNQSVILLSASEDLTDIESATQYAYILSALPKQLITITLNSSG--KQLGLLSTnQ 435
Cdd:smart00327  78 GTNLGAALQYALENlfsksaGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVdeEELKKLAS-A 156

                          170
                   ....*....|....*....
gi 392928328   436 NMFFGVPDYNLTTTIAQQL 454
Cdd:smart00327 157 PGGVYVFLPELLDLLIDLL 175
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 128-276 6.61e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.41  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328  128 PTVPITIlgisNAGQWADVMYALSYTTSNKPQLNDIQQkvSASPNFAMISATDQTPPTLSQMTCRSVSDSTLITTSGPSG 207
Cdd:pfam17823  66 APAPVTL----TKGTSAAHLNSTEVTAEHTPHGTDLSE--PATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPS 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328  208 TTVTVPTTPCASVP-TGPTKTPVTVPTSTGSVSRETKSPVTANPGSTVSTSLSSKPVTVVTQSPrSTTTP 276
Cdd:pfam17823 140 EAFSAPRAAACRANaSAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAP-ATLTP 208
 
Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 481-633 5.83e-10

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: 58.84  E-value: 5.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328 481 TDVTILMDNNNDVGSAmEFQNQCRTIAKLIKTWPISPKLMEGEAIVYSTTdggQIVENPF-SYQSASAFANEVMAFDDYY 559
Cdd:cd01450    1 LDIVFLLDGSESVGPE-NFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDD---VRVEFSLnDYKSKDDLLKAVKNLKYLG 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392928328 560 FAASppSLTASLQYVSQNL---GRRRQSRQQATIVFT--YSSSYSDVQTAIEYVTQIGGNLIIVAVGGADQTVLKQLTG 633
Cdd:cd01450   77 GGGT--NTGKALQYALEQLfseSNARENVPKVIIVLTdgRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIAS 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 285-454 1.06e-08

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: 55.54  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328   285 DVIILLDNSNAMkSFTNFNLVKSwIVKTLLPLWLIDREDVQVAFATYaANDFNTLLDF-DEASEEEVASVISAQMYSGKH 363
Cdd:smart00327   1 DVVFLLDGSGSM-GGNRFELAKE-FVLKLVEQLDIGPDGDRVGLVTF-SDDARVLFPLnDSRSKDALLEALASLSYKLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328   364 NSSITYGIRAAGDI------HGLRPVNQSVILLSASEDLTDIESATQYAYILSALPKQLITITLNSSG--KQLGLLSTnQ 435
Cdd:smart00327  78 GTNLGAALQYALENlfsksaGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVdeEELKKLAS-A 156

                          170
                   ....*....|....*....
gi 392928328   436 NMFFGVPDYNLTTTIAQQL 454
Cdd:smart00327 157 PGGVYVFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
285-453 1.73e-08

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 54.97  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328  285 DVIILLDNSNAMkSFTNFNLVKSWIVKTLLPLwLIDREDVQVAFATYaANDFNTLLDFDEA-SEEEVASVISAQMYSGKH 363
Cdd:pfam00092   1 DIVFLLDGSGSI-GGDNFEKVKEFLKKLVESL-DIGPDGTRVGLVQY-SSDVRTEFPLNDYsSKEELLSAVDNLRYLGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328  364 NSSITYGIRAAGDIH-----GLRP-VNQSVILLSA--SEDlTDIESATQYAY----------ILSALPKQLITITLNSsg 425
Cdd:pfam00092  78 TTNTGKALKYALENLfssaaGARPgAPKVVVLLTDgrSQD-GDPEEVARELKsagvtvfavgVGNADDEELRKIASEP-- 154

                         170       180
                  ....*....|....*....|....*...
gi 392928328  426 kqlgllstNQNMFFGVPDYNLTTTIAQQ 453
Cdd:pfam00092 155 --------GEGHVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 285-404 7.77e-05

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: 43.82  E-value: 7.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328 285 DVIILLDNSNAMKSfTNFNLVKSWIVKTLLPLWlIDREDVQVAFATYA--ANDFNTLLDFDeaSEEEVASVISAQMYSGK 362
Cdd:cd01450    2 DIVFLLDGSESVGP-ENFEKVKDFIEKLVEKLD-IGPDKTRVGLVQYSddVRVEFSLNDYK--SKDDLLKAVKNLKYLGG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 392928328 363 HNSSITYGIRAAGDI----HGLRP-VNQSVILLSA--SEDLTDIESATQ 404
Cdd:cd01450   78 GGTNTGKALQYALEQlfseSNAREnVPKVIIVLTDgrSDDGGDPKEAAA 126
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 128-276 6.61e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.41  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328  128 PTVPITIlgisNAGQWADVMYALSYTTSNKPQLNDIQQkvSASPNFAMISATDQTPPTLSQMTCRSVSDSTLITTSGPSG 207
Cdd:pfam17823  66 APAPVTL----TKGTSAAHLNSTEVTAEHTPHGTDLSE--PATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPS 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328  208 TTVTVPTTPCASVP-TGPTKTPVTVPTSTGSVSRETKSPVTANPGSTVSTSLSSKPVTVVTQSPrSTTTP 276
Cdd:pfam17823 140 EAFSAPRAAACRANaSAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAP-ATLTP 208
motB PRK12799
flagellar motor protein MotB; Reviewed
 134-260 2.20e-03

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 41.24  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328 134 ILGISNAGQWADVMYALSYTTSNKPQLNDIQQKVSASPNFAMISATDQTPP-TLSQMTCRSVSDSTLITTSGPSGTTVTV 212
Cdd:PRK12799 287 ATGLKQIDTHGTVPVAAVTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSaTTTQASAVALSSAGVLPSDVTLPGTVAL 366

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 392928328 213 PTTPCASVPTGPTKTPVTVPTSTGSVSRETKSPVTANPGSTVSTSLSS 260
Cdd:PRK12799 367 PAAEPVNMQPQPMSTTETQQSSTGNITSTANGPTTSLPAAPASNIPVS 414
 
Name Accession Description Interval E-value
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 481-633 5.83e-10

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: 58.84  E-value: 5.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328 481 TDVTILMDNNNDVGSAmEFQNQCRTIAKLIKTWPISPKLMEGEAIVYSTTdggQIVENPF-SYQSASAFANEVMAFDDYY 559
Cdd:cd01450    1 LDIVFLLDGSESVGPE-NFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDD---VRVEFSLnDYKSKDDLLKAVKNLKYLG 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392928328 560 FAASppSLTASLQYVSQNL---GRRRQSRQQATIVFT--YSSSYSDVQTAIEYVTQIGGNLIIVAVGGADQTVLKQLTG 633
Cdd:cd01450   77 GGGT--NTGKALQYALEQLfseSNARENVPKVIIVLTdgRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIAS 153
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 285-454 1.06e-08

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: 55.54  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328   285 DVIILLDNSNAMkSFTNFNLVKSwIVKTLLPLWLIDREDVQVAFATYaANDFNTLLDF-DEASEEEVASVISAQMYSGKH 363
Cdd:smart00327   1 DVVFLLDGSGSM-GGNRFELAKE-FVLKLVEQLDIGPDGDRVGLVTF-SDDARVLFPLnDSRSKDALLEALASLSYKLGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328   364 NSSITYGIRAAGDI------HGLRPVNQSVILLSASEDLTDIESATQYAYILSALPKQLITITLNSSG--KQLGLLSTnQ 435
Cdd:smart00327  78 GTNLGAALQYALENlfsksaGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVdeEELKKLAS-A 156

                          170
                   ....*....|....*....
gi 392928328   436 NMFFGVPDYNLTTTIAQQL 454
Cdd:smart00327 157 PGGVYVFLPELLDLLIDLL 175
VWA pfam00092
von Willebrand factor type A domain;
285-453 1.73e-08

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 54.97  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328  285 DVIILLDNSNAMkSFTNFNLVKSWIVKTLLPLwLIDREDVQVAFATYaANDFNTLLDFDEA-SEEEVASVISAQMYSGKH 363
Cdd:pfam00092   1 DIVFLLDGSGSI-GGDNFEKVKEFLKKLVESL-DIGPDGTRVGLVQY-SSDVRTEFPLNDYsSKEELLSAVDNLRYLGGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328  364 NSSITYGIRAAGDIH-----GLRP-VNQSVILLSA--SEDlTDIESATQYAY----------ILSALPKQLITITLNSsg 425
Cdd:pfam00092  78 TTNTGKALKYALENLfssaaGARPgAPKVVVLLTDgrSQD-GDPEEVARELKsagvtvfavgVGNADDEELRKIASEP-- 154

                         170       180
                  ....*....|....*....|....*...
gi 392928328  426 kqlgllstNQNMFFGVPDYNLTTTIAQQ 453
Cdd:pfam00092 155 --------GEGHVFTVSDFEALEDLQDQ 174
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 285-404 7.77e-05

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: 43.82  E-value: 7.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328 285 DVIILLDNSNAMKSfTNFNLVKSWIVKTLLPLWlIDREDVQVAFATYA--ANDFNTLLDFDeaSEEEVASVISAQMYSGK 362
Cdd:cd01450    2 DIVFLLDGSESVGP-ENFEKVKDFIEKLVEKLD-IGPDKTRVGLVQYSddVRVEFSLNDYK--SKDDLLKAVKNLKYLGG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 392928328 363 HNSSITYGIRAAGDI----HGLRP-VNQSVILLSA--SEDLTDIESATQ 404
Cdd:cd01450   78 GGTNTGKALQYALEQlfseSNAREnVPKVIIVLTDgrSDDGGDPKEAAA 126
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 285-425 2.08e-04

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: 42.55  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328 285 DVIILLDNSNAMKSfTNFNLVKSwIVKTLLPLWLIDREDVQVAFATYAANDFNTLLDFDEASEEEVASVISAQMYSGKHN 364
Cdd:cd00198    2 DIVFLLDVSGSMGG-EKLDKAKE-ALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392928328 365 SSITYGIRAAGDI---HGLRPVNQSVILLSASEDLTDIESATQYAYILSALPKQLITITLNSSG 425
Cdd:cd00198   80 TNIGAALRLALELlksAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDA 143
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 128-276 6.61e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.41  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328  128 PTVPITIlgisNAGQWADVMYALSYTTSNKPQLNDIQQkvSASPNFAMISATDQTPPTLSQMTCRSVSDSTLITTSGPSG 207
Cdd:pfam17823  66 APAPVTL----TKGTSAAHLNSTEVTAEHTPHGTDLSE--PATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPS 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328  208 TTVTVPTTPCASVP-TGPTKTPVTVPTSTGSVSRETKSPVTANPGSTVSTSLSSKPVTVVTQSPrSTTTP 276
Cdd:pfam17823 140 EAFSAPRAAACRANaSAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAP-ATLTP 208
motB PRK12799
flagellar motor protein MotB; Reviewed
 134-260 2.20e-03

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 41.24  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328 134 ILGISNAGQWADVMYALSYTTSNKPQLNDIQQKVSASPNFAMISATDQTPP-TLSQMTCRSVSDSTLITTSGPSGTTVTV 212
Cdd:PRK12799 287 ATGLKQIDTHGTVPVAAVTPSSAVTQSSAITPSSAAIPSPAVIPSSVTTQSaTTTQASAVALSSAGVLPSDVTLPGTVAL 366

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 392928328 213 PTTPCASVPTGPTKTPVTVPTSTGSVSRETKSPVTANPGSTVSTSLSS 260
Cdd:PRK12799 367 PAAEPVNMQPQPMSTTETQQSSTGNITSTANGPTTSLPAAPASNIPVS 414
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 482-621 3.60e-03

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: 39.29  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392928328 482 DVTILMDNNNDVGSAMEFQNQCRTIAKLIKTWPISPKLMEGEAIVYSTTDGGQIVENPFSYQSASAFANEVMAFDDYYFA 561
Cdd:cd01471    2 DLYLLVDGSGSIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALNAIRALLSLYYP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392928328 562 ASPPSLTASLQYVSQNLGRRRQSRQQA---TIVFTYSSSYSDVQT--AIEYVTQIGGNLIIVAVG 621
Cdd:cd01471   82 NGSTNTTSALLVVEKHLFDTRGNRENApqlVIIMTDGIPDSKFRTlkEARKLRERGVIIAVLGVG 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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