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Conserved domains on  [gi|71983551|ref|NP_509176|]
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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
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 158-315 1.11e-68

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: 218.81  E-value: 1.11e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 158 SDIIFVIDATSSVRGIFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEKKQRTKIKLGEHKDRGSLVKAVDELPFFSGIT 237
Cdd:cd01476   1 LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 238 ATGQALKFAANHT---EGRRENFTLNYVILTDGYSYDLIESGARVLREVPNSAIYAVSIGEI--FLRKELEMITGNPDNV 312
Cdd:cd01476  81 ATGAAIEVALQQLdpsEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTGDPgtVDTEELHSITGNEDHI 160


                ...
gi 71983551 313 LTG 315
Cdd:cd01476 161 FTD 163
VWA pfam00092
von Willebrand factor type A domain;
391-555 1.10e-33

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 126.24  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   391 DIGIIFDSSGSL-EKNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDR-SPFYSGTTF 468
Cdd:pfam00092   1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNlRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   469 TNQALKKMAALYEESK---RPNAKLKLMLFTDGYSAE-DTSEGEEALKSQGVVVYTVGISTDksaglNMKELRGMAT--S 542
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNA-----DDEELRKIASepG 155

                         170
                  ....*....|...
gi 71983551   543 SEHYYDSSDFADL 555
Cdd:pfam00092 156 EGHVFTVSDFEAL 168
 
Name Accession Description Interval E-value
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 158-315 1.11e-68

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: 218.81  E-value: 1.11e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 158 SDIIFVIDATSSVRGIFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEKKQRTKIKLGEHKDRGSLVKAVDELPFFSGIT 237
Cdd:cd01476   1 LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 238 ATGQALKFAANHT---EGRRENFTLNYVILTDGYSYDLIESGARVLREVPNSAIYAVSIGEI--FLRKELEMITGNPDNV 312
Cdd:cd01476  81 ATGAAIEVALQQLdpsEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTGDPgtVDTEELHSITGNEDHI 160


                ...
gi 71983551 313 LTG 315
Cdd:cd01476 161 FTD 163
VWA pfam00092
von Willebrand factor type A domain;
391-555 1.10e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 126.24  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   391 DIGIIFDSSGSL-EKNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDR-SPFYSGTTF 468
Cdd:pfam00092   1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNlRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   469 TNQALKKMAALYEESK---RPNAKLKLMLFTDGYSAE-DTSEGEEALKSQGVVVYTVGISTDksaglNMKELRGMAT--S 542
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNA-----DDEELRKIASepG 155

                         170
                  ....*....|...
gi 71983551   543 SEHYYDSSDFADL 555
Cdd:pfam00092 156 EGHVFTVSDFEAL 168
VWA pfam00092
von Willebrand factor type A domain;
159-311 3.78e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 118.92  E-value: 3.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   159 DIIFVIDATSSVRG-IFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEkkQRTKIKLGEHKDRGSLVKAVDELPFFSGIT 237
Cdd:pfam00092   1 DIVFLLDGSGSIGGdNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSD--VRTEFPLNDYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   238 A-TGQALKFAANH----TEGRRENFTLNYVILTDGYSYDL-IESGARVLREVpNSAIYAVSIGEIFLrKELEMITGNPDN 311
Cdd:pfam00092  79 TnTGKALKYALENlfssAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSA-GVTVFAVGVGNADD-EELRKIASEPGE 156
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 391-557 1.24e-30

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: 117.56  E-value: 1.24e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551    391 DIGIIFDSSGSL-EKNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDR-SPFYSGTTF 468
Cdd:smart00327   1 DVVFLLDGSGSMgGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASlSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551    469 TNQALKKMAALYEESK---RPNAKLKLMLFTDGYS---AEDTSEGEEALKSQGVVVYTVGISTDksagLNMKELRGMA-- 540
Cdd:smart00327  81 LGAALQYALENLFSKSagsRRGAPKVVILITDGESndgPKDLLKAAKELKRSGVKVFVVGVGND----VDEEELKKLAsa 156

                          170
                   ....*....|....*..
gi 71983551    541 TSSEHYYDSSDFADLLK 557
Cdd:smart00327 157 PGGVYVFLPELLDLLID 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 390-547 1.93e-29

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: 113.93  E-value: 1.93e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 390 YDIGIIFDSSGSL-EKNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDRSPFYSGT-T 467
Cdd:cd01450   1 LDIVFLLDGSESVgPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 468 FTNQALKKMAALY--EESKRPNAKLKLMLFTDGYSAEDTSEGEEA--LKSQGVVVYTVGISTdksagLNMKELRGMATSS 543
Cdd:cd01450  81 NTGKALQYALEQLfsESNARENVPKVIIVLTDGRSDDGGDPKEAAakLKDEGIKVFVVGVGP-----ADEEELREIASCP 155


                ....
gi 71983551 544 EHYY 547
Cdd:cd01450 156 SERH 159
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 159-312 1.49e-26

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: 1.49e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551    159 DIIFVIDATSSVRGI-FEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEkkQRTKIKLGEHKDRGSLVKAVDELPFF-SGI 236
Cdd:smart00327   1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDD--ARVLFPLNDSRSKDALLEALASLSYKlGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551    237 TATGQALKFAANH----TEGRRENFTLNYVILTDGYSYDLIESGARVLREVPNS--AIYAVSIGEIFLRKELEMITGNPD 310
Cdd:smart00327  79 TNLGAALQYALENlfskSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSgvKVFVVGVGNDVDEEELKKLASAPG 158


                   ..
gi 71983551    311 NV 312
Cdd:smart00327 159 GV 160
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 378-555 1.16e-15

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: 77.29  E-value: 1.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 378 TPEKRGPVKDCIYDIGIIFDSSGSLEKnfQKQLAFAK----QLVEQMPISDnatRVGIVQFAGKtkVRVLANFSQNKSQL 453
Cdd:COG1240  81 LAPLALARPQRGRDVVLVVDASGSMAA--ENRLEAAKgallDFLDDYRPRD---RVGLVAFGGE--AEVLLPLTRDREAL 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 454 KTIIDRSPFySGTTFTNQALKKMAALYEESKRPNAKLkLMLFTDGY---SAEDTSEGEEALKSQGVVVYTVGISTDksaG 530
Cdd:COG1240 154 KRALDELPP-GGGTPLGDALALALELLKRADPARRKV-IVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTE---A 228

                       170       180
                ....*....|....*....|....*.
gi 71983551 531 LNMKELRGMATSSE-HYYDSSDFADL 555
Cdd:COG1240 229 VDEGLLREIAEATGgRYFRADDLSEL 254
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 392-564 1.85e-06

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 50.00  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   392 IGIIFDSSGSLEKNFQKQLAFAKQLVEQ-MPISDnatRVGIVQFAgkTKVRVLANFSQNKSQLKTIIDR----SPFYSGT 466
Cdd:TIGR03436  56 VGLVIDTSGSMRNDLDRARAAAIRFLKTvLRPND---RVFVVTFN--TRLRLLQDFTSDPRLLEAALNRlkppLRTDYNS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   467 TFTNQALKKMAALY--------EESKRPNAKLK----LMLFTDGYSAE-DTSEGE--EALKSQGVVVYTVGISTDKSAGL 531
Cdd:TIGR03436 131 SGAFVRDGGGTALYdaitlaalEQLANALAGIPgrkaLIVISDGGDNRsRDTLERaiDAAQRADVAIYSIDARGLRAPDL 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 71983551   532 N---------MKELRGMA--TSSEHYY-DSSDFADLLKHF---PSSQY 564
Cdd:TIGR03436 211 GagakaglggPEALERLAeeTGGRAFYvNSNDLDGAFAQIaeeLRSQY 258
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 391-559 7.60e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.73  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551  391 DIGIIFDSSGSLEKN--FQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTK--VRVLANFSQNKSQLKTIID--RSPF-- 462
Cdd:PTZ00441  44 DLYLLVDGSGSIGYHnwITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTelIRLGSGASKDKEQALIIVKslRKTYlp 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551  463 YSGTTFTNQALKKMAALYEESKRPNAKLKLMLFTDGY--SAEDTSEGEEALKSQGVVVYTVGISTdksaGLNMKELRGMA 540
Cdd:PTZ00441 124 YGKTNMTDALLEVRKHLNDRVNRENAIQLVILMTDGIpnSKYRALEESRKLKDRNVKLAVIGIGQ----GINHQFNRLLA 199

                        170       180
                 ....*....|....*....|....*..
gi 71983551  541 -----TSSEHYYDSSDFAD---LLKHF 559
Cdd:PTZ00441 200 gcrprEGKCKFYSDADWEEaknLIKPF 226
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 111-295 9.42e-04

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: 41.46  E-value: 9.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 111 GDTEGSGSGDKSGTEESFDASGAQGDSLPDIMKAMDSEAEVLGVNCPSDIIFVIDATSSVRGifEQYITYIEKVVEGL-- 188
Cdd:COG1240  46 GLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAA--ENRLEAAKGALLDFld 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 189 DVQPTvDHVGAIVYSSekkqRTKIKLGEHKDRGSLVKAVDELPFFSGiTATGQALKFAANHTEGRRENFTLNYVILTDGY 268
Cdd:COG1240 124 DYRPR-DRVGLVAFGG----EAEVLLPLTRDREALKRALDELPPGGG-TPLGDALALALELLKRADPARRKVIVLLTDGR 197

                       170       180       190
                ....*....|....*....|....*....|.
gi 71983551 269 ----SYDLIESgARVLREvPNSAIYAVSIGE 295
Cdd:COG1240 198 dnagRIDPLEA-AELAAA-AGIRIYTIGVGT 226
 
Name Accession Description Interval E-value
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 158-315 1.11e-68

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: 218.81  E-value: 1.11e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 158 SDIIFVIDATSSVRGIFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEKKQRTKIKLGEHKDRGSLVKAVDELPFFSGIT 237
Cdd:cd01476   1 LDLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 238 ATGQALKFAANHT---EGRRENFTLNYVILTDGYSYDLIESGARVLREVPNSAIYAVSIGEI--FLRKELEMITGNPDNV 312
Cdd:cd01476  81 ATGAAIEVALQQLdpsEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVPNIETFAVGTGDPgtVDTEELHSITGNEDHI 160


                ...
gi 71983551 313 LTG 315
Cdd:cd01476 161 FTD 163
VWA pfam00092
von Willebrand factor type A domain;
391-555 1.10e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 126.24  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   391 DIGIIFDSSGSL-EKNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDR-SPFYSGTTF 468
Cdd:pfam00092   1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNlRYLGGGTTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   469 TNQALKKMAALYEESK---RPNAKLKLMLFTDGYSAE-DTSEGEEALKSQGVVVYTVGISTDksaglNMKELRGMAT--S 542
Cdd:pfam00092  81 TGKALKYALENLFSSAagaRPGAPKVVVLLTDGRSQDgDPEEVARELKSAGVTVFAVGVGNA-----DDEELRKIASepG 155

                         170
                  ....*....|...
gi 71983551   543 SEHYYDSSDFADL 555
Cdd:pfam00092 156 EGHVFTVSDFEAL 168
VWA pfam00092
von Willebrand factor type A domain;
159-311 3.78e-31

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 118.92  E-value: 3.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   159 DIIFVIDATSSVRG-IFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEkkQRTKIKLGEHKDRGSLVKAVDELPFFSGIT 237
Cdd:pfam00092   1 DIVFLLDGSGSIGGdNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSD--VRTEFPLNDYSSKEELLSAVDNLRYLGGGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   238 A-TGQALKFAANH----TEGRRENFTLNYVILTDGYSYDL-IESGARVLREVpNSAIYAVSIGEIFLrKELEMITGNPDN 311
Cdd:pfam00092  79 TnTGKALKYALENlfssAAGARPGAPKVVVLLTDGRSQDGdPEEVARELKSA-GVTVFAVGVGNADD-EELRKIASEPGE 156
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 391-557 1.24e-30

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: 117.56  E-value: 1.24e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551    391 DIGIIFDSSGSL-EKNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDR-SPFYSGTTF 468
Cdd:smart00327   1 DVVFLLDGSGSMgGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASlSYKLGGGTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551    469 TNQALKKMAALYEESK---RPNAKLKLMLFTDGYS---AEDTSEGEEALKSQGVVVYTVGISTDksagLNMKELRGMA-- 540
Cdd:smart00327  81 LGAALQYALENLFSKSagsRRGAPKVVILITDGESndgPKDLLKAAKELKRSGVKVFVVGVGND----VDEEELKKLAsa 156

                          170
                   ....*....|....*..
gi 71983551    541 TSSEHYYDSSDFADLLK 557
Cdd:smart00327 157 PGGVYVFLPELLDLLID 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 390-547 1.93e-29

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: 113.93  E-value: 1.93e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 390 YDIGIIFDSSGSL-EKNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDRSPFYSGT-T 467
Cdd:cd01450   1 LDIVFLLDGSESVgPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 468 FTNQALKKMAALY--EESKRPNAKLKLMLFTDGYSAEDTSEGEEA--LKSQGVVVYTVGISTdksagLNMKELRGMATSS 543
Cdd:cd01450  81 NTGKALQYALEQLfsESNARENVPKVIIVLTDGRSDDGGDPKEAAakLKDEGIKVFVVGVGP-----ADEEELREIASCP 155


                ....
gi 71983551 544 EHYY 547
Cdd:cd01450 156 SERH 159
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 159-310 9.25e-27

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: 106.22  E-value: 9.25e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 159 DIIFVIDATSSVR-GIFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEkkQRTKIKLGEHKDRGSLVKAVDELPFFSGI- 236
Cdd:cd01450   2 DIVFLLDGSESVGpENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDD--VRVEFSLNDYKSKDDLLKAVKNLKYLGGGg 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983551 237 TATGQALKFAANH---TEGRRENFTLNYVILTDGYSYDL--IESGARVLREvPNSAIYAVSIGEiFLRKELEMITGNPD 310
Cdd:cd01450  80 TNTGKALQYALEQlfsESNARENVPKVIIVLTDGRSDDGgdPKEAAAKLKD-EGIKVFVVGVGP-ADEEELREIASCPS 156
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 159-312 1.49e-26

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: 1.49e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551    159 DIIFVIDATSSVRGI-FEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEkkQRTKIKLGEHKDRGSLVKAVDELPFF-SGI 236
Cdd:smart00327   1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDD--ARVLFPLNDSRSKDALLEALASLSYKlGGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551    237 TATGQALKFAANH----TEGRRENFTLNYVILTDGYSYDLIESGARVLREVPNS--AIYAVSIGEIFLRKELEMITGNPD 310
Cdd:smart00327  79 TNLGAALQYALENlfskSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSgvKVFVVGVGNDVDEEELKKLASAPG 158


                   ..
gi 71983551    311 NV 312
Cdd:smart00327 159 GV 160
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 390-547 2.28e-25

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 102.26  E-value: 2.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 390 YDIGIIFDSSGSLEK-NFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDRSPFY-SGTT 467
Cdd:cd00198   1 ADIVFLLDVSGSMGGeKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGlGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 468 FTNQALKKMAALYEESKRPNAKLKLMLFTDGYSAEDTSEGEEA---LKSQGVVVYTVGISTDKsaglNMKELRGMA--TS 542
Cdd:cd00198  81 NIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAareLRKLGITVYTIGIGDDA----NEDELKEIAdkTT 156


                ....*
gi 71983551 543 SEHYY 547
Cdd:cd00198 157 GGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 391-545 5.68e-25

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: 101.32  E-value: 5.68e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 391 DIGIIFDSSGSLEKNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANF--SQNKSQLKTIIDRSPFYSGTTF 468
Cdd:cd01476   2 DLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLpkHNDGEELLEKVDNLRFIGGTTA 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983551 469 TNQALKKMAALYEES--KRPNAKLKLMLFTDGYSAEDTSEGEEALKSQgVVVYTVGISTDKSAGLNMKELRGMATSSEH 545
Cdd:cd01476  82 TGAAIEVALQQLDPSegRREGIPKVVVVLTDGRSHDDPEKQARILRAV-PNIETFAVGTGDPGTVDTEELHSITGNEDH 159
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 159-309 2.73e-23

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: 96.53  E-value: 2.73e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 159 DIIFVIDATSSV-RGIFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEkkQRTKIKLGEHKDRGSLVKAVDELPFFSGIT 237
Cdd:cd01472   2 DIVFLVDGSESIgLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDD--PRTEFYLNTYRSKDDVLEAVKNLRYIGGGT 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983551 238 ATGQALKFAANH----TEGRRENFTLNYVILTDGYSYDLIESGARVLREVpNSAIYAVSIGEiFLRKELEMITGNP 309
Cdd:cd01472  80 NTGKALKYVRENlfteASGSREGVPKVLVVITDGKSQDDVEEPAVELKQA-GIEVFAVGVKN-ADEEELKQIASDP 153
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 391-533 2.85e-21

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: 90.75  E-value: 2.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 391 DIGIIFDSSGSL-EKNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDRSPFYSGTTFT 469
Cdd:cd01472   2 DIVFLVDGSESIgLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983551 470 NQALKKMAA-LYEESKRP--NAKLKLMLFTDGYSAEDTSEGEEALKSQGVVVYTVGISTDKSAGLNM 533
Cdd:cd01472  82 GKALKYVREnLFTEASGSreGVPKVLVVITDGKSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQ 148
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 159-310 2.98e-21

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: 90.81  E-value: 2.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 159 DIIFVIDATSSV-RGIFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEKkqRTKIKLGEHKDRGSLVKAVDELPFFSGIT 237
Cdd:cd01482   2 DIVFLVDGSWSIgRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDP--RTEFDLNAYTSKEDVLAAIKNLPYKGGNT 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983551 238 ATGQALKFAANHT----EGRRENFTLNYVILTDGYSYDLIESGARVLREVPNSaIYAVSIGEIfLRKELEMITGNPD 310
Cdd:cd01482  80 RTGKALTHVREKNftpdAGARPGVPKVVILITDGKSQDDVELPARVLRNLGVN-VFAVGVKDA-DESELKMIASKPS 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 159-311 1.13e-17

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: 80.30  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 159 DIIFVIDATSSVRG-IFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSekKQRTKIKLGEHKDRGSLVKAVDELPF-FSGI 236
Cdd:cd00198   2 DIVFLLDVSGSMGGeKLDKAKEALKALVSSLSASPPGDRVGLVTFGS--NARVVLPLTTDTDKADLLEAIDALKKgLGGG 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983551 237 TATGQALKFAANHTEGRRENFTLNYVIL-TDGYSYDLIESGARVLREV--PNSAIYAVSIGEIFLRKELEMITGNPDN 311
Cdd:cd00198  80 TNIGAALRLALELLKSAKRPNARRVIILlTDGEPNDGPELLAEAARELrkLGITVYTIGIGDDANEDELKEIADKTTG 157
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 157-309 2.01e-17

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: 81.28  E-value: 2.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 157 PSDIIFVIDATSSVRGI-FEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEKKQrtKIKLGEHKDRGSLVKAVDELPFFSG 235
Cdd:cd01475   2 PTDLVFLIDSSRSVRPEnFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQ--EFPLGRFKSKADLKRAVRRMEYLET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 236 ITATGQALKFAANHT----EGRR---ENFTLNYVILTDGYSYDLIESGARVLREVpNSAIYAVSIGEIFLrKELEMITGN 308
Cdd:cd01475  80 GTMTGLAIQYAMNNAfseaEGARpgsERVPRVGIVVTDGRPQDDVSEVAAKARAL-GIEMFAVGVGRADE-EELREIASE 157


                .
gi 71983551 309 P 309
Cdd:cd01475 158 P 158
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 391-556 5.35e-16

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: 76.27  E-value: 5.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 391 DIGIIFDSSGSL-EKN-FQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKV--RVLANFSQNKSQLKTIID--RSPFYS 464
Cdd:cd01471   2 DLYLLVDGSGSIgYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKEliRLSSPNSTNKDLALNAIRalLSLYYP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 465 -GTTFTNQALKKMAALYEESK--RPNAKLKLMLFTDGYSA--EDTSEGEEALKSQGVVVYTVGISTdksaGLNMKELRGM 539
Cdd:cd01471  82 nGSTNTTSALLVVEKHLFDTRgnRENAPQLVIIMTDGIPDskFRTLKEARKLRERGVIIAVLGVGQ----GVNHEENRSL 157

                       170       180
                ....*....|....*....|..
gi 71983551 540 A-----TSSEHYYDSSDFADLL 556
Cdd:cd01471 158 VgcdpdDSPCPLYLQSSWSEVQ 179
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 383-556 6.93e-16

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: 75.88  E-value: 6.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 383 GPVkdciyDIGIIFDSSGSL-EKNFQKQLAFAKQLVEQM------PISDNATRVGIVQFAGKTKV-RVLANFSQNKSQLK 454
Cdd:cd01480   1 GPV-----DITFVLDSSESVgLQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVeAGFLRDIRNYTSLK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 455 TIIDRSPFYSGTTFTNQALKKMAALYEESKRPNAKLKLMLFTDGYSAEDTSEG-EEAL---KSQGVVVYTVGISTDKSAG 530
Cdd:cd01480  76 EAVDNLEYIGGGTFTDCALKYATEQLLEGSHQKENKFLLVITDGHSDGSPDGGiEKAVneaDHLGIKIFFVAVGSQNEEP 155

                       170       180
                ....*....|....*....|....*.
gi 71983551 531 LNmkelRGMATSSEHYYDSSdFADLL 556
Cdd:cd01480 156 LS----RIACDGKSALYREN-FAELL 176
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 378-555 1.16e-15

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: 77.29  E-value: 1.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 378 TPEKRGPVKDCIYDIGIIFDSSGSLEKnfQKQLAFAK----QLVEQMPISDnatRVGIVQFAGKtkVRVLANFSQNKSQL 453
Cdd:COG1240  81 LAPLALARPQRGRDVVLVVDASGSMAA--ENRLEAAKgallDFLDDYRPRD---RVGLVAFGGE--AEVLLPLTRDREAL 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 454 KTIIDRSPFySGTTFTNQALKKMAALYEESKRPNAKLkLMLFTDGY---SAEDTSEGEEALKSQGVVVYTVGISTDksaG 530
Cdd:COG1240 154 KRALDELPP-GGGTPLGDALALALELLKRADPARRKV-IVLLTDGRdnaGRIDPLEAAELAAAAGIRIYTIGVGTE---A 228

                       170       180
                ....*....|....*....|....*.
gi 71983551 531 LNMKELRGMATSSE-HYYDSSDFADL 555
Cdd:COG1240 229 VDEGLLREIAEATGgRYFRADDLSEL 254
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 391-552 4.32e-14

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: 70.01  E-value: 4.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 391 DIGIIFDSSGSLEK-NFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRV-LANFSQNKSQLKTiIDRSPFYSGTTF 468
Cdd:cd01482   2 DIVFLVDGSWSIGRsNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFdLNAYTSKEDVLAA-IKNLPYKGGNTR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 469 TNQALKKMA--ALYEES-KRPNAKLKLMLFTDGYSAEDTSEGEEALKSQGVVVYTVGIstdKSAglNMKELRGMA--TSS 543
Cdd:cd01482  81 TGKALTHVRekNFTPDAgARPGVPKVVILITDGKSQDDVELPARVLRNLGVNVFAVGV---KDA--DESELKMIAskPSE 155


                ....*....
gi 71983551 544 EHYYDSSDF 552
Cdd:cd01482 156 THVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 391-552 1.28e-13

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: 70.49  E-value: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 391 DIGIIFDSSGSL-EKNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRV-LANFSQnKSQLKTIIDRSPFYSGTTF 468
Cdd:cd01475   4 DLVFLIDSSRSVrPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFpLGRFKS-KADLKRAVRRMEYLETGTM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 469 TNQALKKMA--ALYE-ESKRP---NAKLKLMLFTDGYSAEDTSEGEEALKSQGVVVYTVGISTdksagLNMKELRGMAT- 541
Cdd:cd01475  83 TGLAIQYAMnnAFSEaEGARPgseRVPRVGIVVTDGRPQDDVSEVAAKARALGIEMFAVGVGR-----ADEEELREIASe 157

                       170
                ....*....|..
gi 71983551 542 -SSEHYYDSSDF 552
Cdd:cd01475 158 pLADHVFYVEDF 169
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 391-556 1.34e-12

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: 66.23  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 391 DIGIIFDSSGSLE-KNFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDRSPFYSGTTFT 469
Cdd:cd01469   2 DIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 470 NQALKKMAA-LYEESK--RPNAKLKLMLFTDGYSaEDTSEGEEALKS---QGVVVYTVGI----STDKSaglnMKELRGM 539
Cdd:cd01469  82 ATAIQYVVTeLFSESNgaRKDATKVLVVITDGES-HDDPLLKDVIPQaerEGIIRYAIGVgghfQRENS----REELKTI 156

                       170
                ....*....|....*....
gi 71983551 540 AT--SSEHYYDSSDFADLL 556
Cdd:cd01469 157 ASkpPEEHFFNVTDFAALK 175
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 156-270 3.69e-12

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: 65.10  E-value: 3.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 156 CPSDIIFVIDATSSVrGI--FEQYITYIEKVVE------GLDVQPTVDHVGAIVYSSEKKQrTKIKLGEHKDRGSLVKAV 227
Cdd:cd01480   1 GPVDITFVLDSSESV-GLqnFDITKNFVKRVAErflkdyYRKDPAGSWRVGVVQYSDQQEV-EAGFLRDIRNYTSLKEAV 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71983551 228 DELPFFSGITATGQALKFAANHTEGRRENFTLNYVIL-TDGYSY 270
Cdd:cd01480  79 DNLEYIGGGTFTDCALKYATEQLLEGSHQKENKFLLViTDGHSD 122
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 159-314 8.66e-12

VWA_collagen alpha 3(VI) like: 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: 238758  Cd Length: 165  Bit Score: 63.50  E-value: 8.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 159 DIIFVIDATSSVRGIFEQYI-TYIEKVVEGLDVQPTVDHVGAIVYSSEKkqRTKIKLGEHKDRGSLVKAVDELPFFSGIT 237
Cdd:cd01481   2 DIVFLIDGSDNVGSGNFPAIrDFIERIVQSLDVGPDKIRVAVVQFSDTP--RPEFYLNTHSTKADVLGAVRRLRLRGGSQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 238 A-TGQALKFAANH----TEGRR--ENFTLNYVILTDGYSYDLIESGARVLREvpnSAIYAVSIGEIFL-RKELEMITGNP 309
Cdd:cd01481  80 LnTGSALDYVVKNlftkSAGSRieEGVPQFLVLITGGKSQDDVERPAVALKR---AGIVPFAIGARNAdLAELQQIAFDP 156


                ....*
gi 71983551 310 DNVLT 314
Cdd:cd01481 157 SFVFQ 161
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 158-310 4.45e-11

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: 61.99  E-value: 4.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 158 SDIIFVIDATSSVR-GIFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEkkQRTKIKLGEHKDRGSLVKAVDELPFFSGI 236
Cdd:cd01469   1 MDIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSES--FRTEFTLNEYRTKEEPLSLVKHISQLLGL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 237 TATGQALKFAA----NHTEGRRENFTLNYVILTDGYSYD------LIES--GARVLRevpnsaiYAVSIGEIFLRK---- 300
Cdd:cd01469  79 TNTATAIQYVVtelfSESNGARKDATKVLVVITDGESHDdpllkdVIPQaeREGIIR-------YAIGVGGHFQREnsre 151

                       170
                ....*....|
gi 71983551 301 ELEMITGNPD 310
Cdd:cd01469 152 ELKTIASKPP 161
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 390-525 1.64e-10

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 60.41  E-value: 1.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 390 YDIGIIFDSSGSLEKNFQKQ--LAFAKQLVEQMPISDNATRVGIVQFAGktKVRVLANFSQNKSQ-----LKTI--IDRS 460
Cdd:cd01473   1 YDLTLILDESASIGYSNWRKdvIPFTEKIINNLNISKDKVHVGILLFAE--KNRDVVPFSDEERYdknelLKKIndLKNS 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71983551 461 PFYSGTTFTNQALKkmAALYEESKRPNAKLKL----MLFTDGysaEDTSEGEEAL-------KSQGVVVYTVGIST 525
Cdd:cd01473  79 YRSGGETYIVEALK--YGLKNYTKHGNRRKDApkvtMLFTDG---NDTSASKKELqdisllyKEENVKLLVVGVGA 149
VWA_2 pfam13519
von Willebrand factor type A domain;
394-495 1.82e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.99  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   394 IIFDSSGS------LEKNFQKQLAFAKQLVEQMPISdnatRVGIVQFAGKtkVRVLANFSQNKSQLKTIIDRSPFYSGTT 467
Cdd:pfam13519   3 FVLDTSGSmrngdyGPTRLEAAKDAVLALLKSLPGD----RVGLVTFGDG--PEVLIPLTKDRAKILRALRRLEPKGGGT 76

                          90       100
                  ....*....|....*....|....*...
gi 71983551   468 FTNQALkKMAALYEESKRPNAKLKLMLF 495
Cdd:pfam13519  77 NLAAAL-QLARAALKHRRKNQPRRIVLI 103
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 389-551 7.47e-07

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: 49.82  E-value: 7.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 389 IYDIGIIFDSSGSLEKNFQKQLAFAKQLVEQMpISDNaTRVGIVQFAGK-TKVRVLANFSQNKSQLKTIIDR-SPfySGT 466
Cdd:cd01474   4 HFDLYFVLDKSGSVAANWIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRaTKILPLTDDSSAIIKGLEVLKKvTP--SGQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 467 TFTNQALKKMAALYEESKRPNAKLK--LMLFTDGYSAED--TSEGEEA--LKSQGVVVYTVGIStdksaGLNMKELRGMA 540
Cdd:cd01474  80 TYIHEGLENANEQIFNRNGGGRETVsvIIALTDGQLLLNghKYPEHEAklSRKLGAIVYCVGVT-----DFLKSQLINIA 154

                       170
                ....*....|.
gi 71983551 541 TSSEHYYDSSD 551
Cdd:cd01474 155 DSKEYVFPVTS 165
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 391-552 1.18e-06

VWA_collagen alpha 3(VI) like: 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: 238758  Cd Length: 165  Bit Score: 48.86  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 391 DIGIIFDSSGSLEK-NFQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTKVRVLANFSQNKSQLKTIIDR------SPFY 463
Cdd:cd01481   2 DIVFLIDGSDNVGSgNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRlrlrggSQLN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 464 SG--------TTFTNQALKKMaalyEESKRPNaklkLMLFTDGYSAEDTSEGEEALKSQGVVVYTVGIStdksaGLNMKE 535
Cdd:cd01481  82 TGsaldyvvkNLFTKSAGSRI----EEGVPQF----LVLITGGKSQDDVERPAVALKRAGIVPFAIGAR-----NADLAE 148

                       170
                ....*....|....*..
gi 71983551 536 LRGMATSSEHYYDSSDF 552
Cdd:cd01481 149 LQQIAFDPSFVFQVSDF 165
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 392-564 1.85e-06

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 50.00  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   392 IGIIFDSSGSLEKNFQKQLAFAKQLVEQ-MPISDnatRVGIVQFAgkTKVRVLANFSQNKSQLKTIIDR----SPFYSGT 466
Cdd:TIGR03436  56 VGLVIDTSGSMRNDLDRARAAAIRFLKTvLRPND---RVFVVTFN--TRLRLLQDFTSDPRLLEAALNRlkppLRTDYNS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   467 TFTNQALKKMAALY--------EESKRPNAKLK----LMLFTDGYSAE-DTSEGE--EALKSQGVVVYTVGISTDKSAGL 531
Cdd:TIGR03436 131 SGAFVRDGGGTALYdaitlaalEQLANALAGIPgrkaLIVISDGGDNRsRDTLERaiDAAQRADVAIYSIDARGLRAPDL 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 71983551   532 N---------MKELRGMA--TSSEHYY-DSSDFADLLKHF---PSSQY 564
Cdd:TIGR03436 211 GagakaglggPEALERLAeeTGGRAFYvNSNDLDGAFAQIaeeLRSQY 258
VWA_2 pfam13519
von Willebrand factor type A domain;
160-256 6.79e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 44.98  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551   160 IIFVIDATSSVRG------IFEQYITYIEKVVEGLdvqPTvDHVGAIVYSSEkkqrTKIKLGEHKDRGSLVKAVDELPFF 233
Cdd:pfam13519   1 LVFVLDTSGSMRNgdygptRLEAAKDAVLALLKSL---PG-DRVGLVTFGDG----PEVLIPLTKDRAKILRALRRLEPK 72

                          90       100
                  ....*....|....*....|...
gi 71983551   234 SGITATGQALKFAANHTEGRREN 256
Cdd:pfam13519  73 GGGTNLAAALQLARAALKHRRKN 95
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 159-282 7.39e-06

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: 46.61  E-value: 7.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 159 DIIFVIDATSSVR--GIFEQYITYIEKVVEGLDVQPTVDHVGAIVYSSEKKQRTKIKLGEHKDRGSL---VKAVDELPFF 233
Cdd:cd01471   2 DLYLLVDGSGSIGysNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLAlnaIRALLSLYYP 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 71983551 234 SGITATGQALKFAANH---TEGRRENFTLNYVILTDGYSYDLIES--GARVLRE 282
Cdd:cd01471  82 NGSTNTTSALLVVEKHlfdTRGNRENAPQLVIIMTDGIPDSKFRTlkEARKLRE 135
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 391-559 7.60e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.73  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551  391 DIGIIFDSSGSLEKN--FQKQLAFAKQLVEQMPISDNATRVGIVQFAGKTK--VRVLANFSQNKSQLKTIID--RSPF-- 462
Cdd:PTZ00441  44 DLYLLVDGSGSIGYHnwITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTelIRLGSGASKDKEQALIIVKslRKTYlp 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551  463 YSGTTFTNQALKKMAALYEESKRPNAKLKLMLFTDGY--SAEDTSEGEEALKSQGVVVYTVGISTdksaGLNMKELRGMA 540
Cdd:PTZ00441 124 YGKTNMTDALLEVRKHLNDRVNRENAIQLVILMTDGIpnSKYRALEESRKLKDRNVKLAVIGIGQ----GINHQFNRLLA 199

                        170       180
                 ....*....|....*....|....*..
gi 71983551  541 -----TSSEHYYDSSDFAD---LLKHF 559
Cdd:PTZ00441 200 gcrprEGKCKFYSDADWEEaknLIKPF 226
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 111-295 9.42e-04

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: 41.46  E-value: 9.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 111 GDTEGSGSGDKSGTEESFDASGAQGDSLPDIMKAMDSEAEVLGVNCPSDIIFVIDATSSVRGifEQYITYIEKVVEGL-- 188
Cdd:COG1240  46 GLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAA--ENRLEAAKGALLDFld 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 189 DVQPTvDHVGAIVYSSekkqRTKIKLGEHKDRGSLVKAVDELPFFSGiTATGQALKFAANHTEGRRENFTLNYVILTDGY 268
Cdd:COG1240 124 DYRPR-DRVGLVAFGG----EAEVLLPLTRDREALKRALDELPPGGG-TPLGDALALALELLKRADPARRKVIVLLTDGR 197

                       170       180       190
                ....*....|....*....|....*....|.
gi 71983551 269 ----SYDLIESgARVLREvPNSAIYAVSIGE 295
Cdd:COG1240 198 dnagRIDPLEA-AELAAA-AGIRIYTIGVGT 226
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 426-546 1.02e-03

VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 40.07  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 426 ATRVGIVQFAGKTK-----VRVLANfsqNKSQLKTIIDRSPFYSGTTfTNQALKKMAALYEESKRPNAKLKLMLFTDGYs 500
Cdd:cd01466  35 ADRLSIVTFSTSAKrlsplRRMTAK---GKRSAKRVVDGLQAGGGTN-VVGGLKKALKVLGDRRQKNPVASIMLLSDGQ- 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 71983551 501 aedTSEGEEALKS--QGVVVYTVGISTDKSAGLnMKELRGMATSSEHY 546
Cdd:cd01466 110 ---DNHGAVVLRAdnAPIPIHTFGLGASHDPAL-LAFIAEITGGTFSY 153
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 159-312 1.57e-03

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: 39.80  E-value: 1.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 159 DIIFVIDATSSVRGIFEQYITYIEKVVEGLdVQPTVdHVGAIVYSSekkqRTKIKLGEHKDRGSLVKAVDEL----PffS 234
Cdd:cd01474   6 DLYFVLDKSGSVAANWIEIYDFVEQLVDRF-NSPGL-RFSFITFST----RATKILPLTDDSSAIIKGLEVLkkvtP--S 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983551 235 GITATGQALKFAA-----NHTEGRRENFTLnyVILTDG------YSYDliESGARVLREVpNSAIYAVSIGEiFLRKELE 303
Cdd:cd01474  78 GQTYIHEGLENANeqifnRNGGGRETVSVI--IALTDGqlllngHKYP--EHEAKLSRKL-GAIVYCVGVTD-FLKSQLI 151


                ....*....
gi 71983551 304 MITGNPDNV 312
Cdd:cd01474 152 NIADSKEYV 160
 
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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