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Conserved domains on  [gi|2217275794|ref|XP_047280662|]
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anthrax toxin receptor-like isoform X5 [Homo sapiens]

Protein Classification

VWA domain-containing protein( domain architecture ID 10208431)

VWA (von Willebrand factor type A) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2-159 3.09e-48

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 cd01474:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 185  Bit Score: 165.38  E-value: 3.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   2 WVEETVARFQSPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPDGHTFMQAGFRKAIQQIESFN-SGNKVPSM 80
Cdd:cd01474    27 FVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENANEQIFNRNgGGRETVSV 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217275794  81 IIAMTDGELVAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHVFAVENGFKALRSTIDALTSKVCLDV 159
Cdd:cd01474   107 IIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 154-253 6.57e-47

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


:

Pssm-ID: 461684  Cd Length: 102  Bit Score: 158.95  E-value: 6.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794 154 KVCLDVTSVEPSSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 233
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|
gi 2217275794 234 SLNKGKTFFKSNVSITSTTC 253
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTC 100
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 2-159 3.09e-48

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: 165.38  E-value: 3.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   2 WVEETVARFQSPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPDGHTFMQAGFRKAIQQIESFN-SGNKVPSM 80
Cdd:cd01474    27 FVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENANEQIFNRNgGGRETVSV 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217275794  81 IIAMTDGELVAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHVFAVENGFKALRSTIDALTSKVCLDV 159
Cdd:cd01474   107 IIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 154-253 6.57e-47

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


Pssm-ID: 461684  Cd Length: 102  Bit Score: 158.95  E-value: 6.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794 154 KVCLDVTSVEPSSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 233
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|
gi 2217275794 234 SLNKGKTFFKSNVSITSTTC 253
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTC 100
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 3-151 3.80e-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: 75.36  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   3 VEETVARFQsPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQkivPDGHTFMQAGFRKAIQQIESFNSGNKVpsMII 82
Cdd:COG1240   118 LLDFLDDYR-PRDRVGLVAFGGEAEVLLPLTRDREALKRALDELP---PGGGTPLGDALALALELLKRADPARRK--VIV 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217275794  83 AMTDGElvAHA-FQDTLREAQKARKLGANVYTLGVAD--YNLDQITAIAD-SPGHVFAVENgFKALRSTIDAL 151
Cdd:COG1240   192 LLTDGR--DNAgRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEaTGGRYFRADD-LSELAAIYREI 261
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 3-139 1.14e-14

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: 72.10  E-value: 1.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794    3 VEETVARF--QSPNIRMCFITYSTDGQTVLPL--TSDKNRIKNGLDQLQKiVPDGHTFMQAGFRKAIQQIESFNSGNK-- 76
Cdd:smart00327  24 VLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSY-KLGGGTNLGAALQYALENLFSKSAGSRrg 102

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217275794   77 VPSMIIAMTDGELVAHAfQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIADSPGHVFAVEN 139
Cdd:smart00327 103 APKVVILITDGESNDGP-KDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGGVYVFLP 165
VWA pfam00092
von Willebrand factor type A domain;
3-150 9.77e-14

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 69.23  E-value: 9.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   3 VEETVARFQ--SPNIRMCFITYSTDGQTVLPLTSDKNR--IKNGLDQLqKIVPDGHTFMQAGFRKAIQQI--ESFNSGNK 76
Cdd:pfam00092  24 LKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKeeLLSAVDNL-RYLGGGTTNTGKALKYALENLfsSAAGARPG 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217275794  77 VPSMIIAMTDGElvaHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSP--GHVFAVENgFKALRSTIDA 150
Cdd:pfam00092 103 APKVVVLLTDGR---SQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGHVFTVSD-FEALEDLQDQ 174
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 2-159 3.09e-48

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: 165.38  E-value: 3.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   2 WVEETVARFQSPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPDGHTFMQAGFRKAIQQIESFN-SGNKVPSM 80
Cdd:cd01474    27 FVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENANEQIFNRNgGGRETVSV 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217275794  81 IIAMTDGELVAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHVFAVENGFKALRSTIDALTSKVCLDV 159
Cdd:cd01474   107 IIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 154-253 6.57e-47

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


Pssm-ID: 461684  Cd Length: 102  Bit Score: 158.95  E-value: 6.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794 154 KVCLDVTSVEPSSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 233
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|
gi 2217275794 234 SLNKGKTFFKSNVSITSTTC 253
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTC 100
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2-135 2.38e-18

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: 82.34  E-value: 2.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   2 WVEETVARF-QSPN-IRMCFITYSTDGQTVLPLTSDKNR--IKNGLDQLQKIVPDGhTFMQAGFRKAIQQI-ESFNSGNK 76
Cdd:cd01450    24 FIEKLVEKLdIGPDkTRVGLVQYSDDVRVEFSLNDYKSKddLLKAVKNLKYLGGGG-TNTGKALQYALEQLfSESNAREN 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217275794  77 VPSMIIAMTDGElvAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPG--HVF 135
Cdd:cd01450   103 VPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSerHVF 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 3-151 3.80e-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: 75.36  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   3 VEETVARFQsPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQkivPDGHTFMQAGFRKAIQQIESFNSGNKVpsMII 82
Cdd:COG1240   118 LLDFLDDYR-PRDRVGLVAFGGEAEVLLPLTRDREALKRALDELP---PGGGTPLGDALALALELLKRADPARRK--VIV 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217275794  83 AMTDGElvAHA-FQDTLREAQKARKLGANVYTLGVAD--YNLDQITAIAD-SPGHVFAVENgFKALRSTIDAL 151
Cdd:COG1240   192 LLTDGR--DNAgRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEaTGGRYFRADD-LSELAAIYREI 261
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 12-135 7.71e-15

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: 72.21  E-value: 7.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794  12 SPNIRMCFITYSTDGQTVLPLT--SDKNRIKNGLDQLQKIvPDGHTFMQAGFRKAIQQIESFNSGNkVPSMIIAMTDGEl 89
Cdd:cd00198    36 PPGDRVGLVTFGSNARVVLPLTtdTDKADLLEAIDALKKG-LGGGTNIGAALRLALELLKSAKRPN-ARRVIILLTDGE- 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2217275794  90 VAHAFQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIAD--SPGHVF 135
Cdd:cd00198   113 PNDGPELLAEAARELRKLGITVYTIGIgDDANEDELKEIADktTGGAVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 3-139 1.14e-14

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: 72.10  E-value: 1.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794    3 VEETVARF--QSPNIRMCFITYSTDGQTVLPL--TSDKNRIKNGLDQLQKiVPDGHTFMQAGFRKAIQQIESFNSGNK-- 76
Cdd:smart00327  24 VLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSY-KLGGGTNLGAALQYALENLFSKSAGSRrg 102

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217275794   77 VPSMIIAMTDGELVAHAfQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIADSPGHVFAVEN 139
Cdd:smart00327 103 APKVVILITDGESNDGP-KDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGGVYVFLP 165
VWA pfam00092
von Willebrand factor type A domain;
3-150 9.77e-14

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 69.23  E-value: 9.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   3 VEETVARFQ--SPNIRMCFITYSTDGQTVLPLTSDKNR--IKNGLDQLqKIVPDGHTFMQAGFRKAIQQI--ESFNSGNK 76
Cdd:pfam00092  24 LKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKeeLLSAVDNL-RYLGGGTTNTGKALKYALENLfsSAAGARPG 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217275794  77 VPSMIIAMTDGElvaHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSP--GHVFAVENgFKALRSTIDA 150
Cdd:pfam00092 103 APKVVVLLTDGR---SQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGHVFTVSD-FEALEDLQDQ 174
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 12-129 2.15e-13

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 70.90  E-value: 2.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794  12 SPNIRMCFITYSTDGQTVLPLTS--DKNRIKNGLDQLQkivPDGHTFMQAGFRKAIQQIESFNSGNKVPSMIIaMTDGEL 89
Cdd:COG2304   124 RPGDRVSIVTFAGDARVLLPPTPatDRAKILAAIDRLQ---AGGGTALGAGLELAYELARKHFIPGRVNRVIL-LTDGDA 199

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217275794  90 VAHA--FQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIAD 129
Cdd:COG2304   200 NVGItdPEELLKLAEEAREEGITLTTLGVgSDYNEDLLERLAD 242
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 20-137 5.44e-09

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 55.36  E-value: 5.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794  20 ITYSTDGQTVLPLTS--DKNRIKNGLDQLQkivPDGHTFMQAGFRKAIQQIESfNSGNKVPSMIIAMTDGEL-VAHAFQD 96
Cdd:cd01465    41 VTYDGAAETVLPATPvrDKAAILAAIDRLT---AGGSTAGGAGIQLGYQEAQK-HFVPGGVNRILLATDGDFnVGETDPD 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217275794  97 TLRE-AQKARKLGANVYTLGVAD-YNLDQITAIADSPGHVFAV 137
Cdd:cd01465   117 ELARlVAQKRESGITLSTLGFGDnYNEDLMEAIADAGNGNTAY 159
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 12-119 2.24e-08

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: 53.93  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794  12 SPN-IRMCFITYSTDGQTVLPLTS----DKNRIKNGLDQLQKI-VPDGHTFMQAGFRKAIQQIESFNSG-NKVPSMIIAM 84
Cdd:cd01471    36 SPDeINLYLVTFSTNAKELIRLSSpnstNKDLALNAIRALLSLyYPNGSTNTTSALLVVEKHLFDTRGNrENAPQLVIIM 115

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217275794  85 TDGElvAHAFQDTLREAQKARKLGANVYTLGVADY 119
Cdd:cd01471   116 TDGI--PDSKFRTLKEARKLRERGVIIAVLGVGQG 148
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 3-139 8.77e-07

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: 48.76  E-value: 8.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   3 VEETVARF-QSPN-IRMCFITYSTDGQTVLPLT--SDKNRIKNGLDQLQKIvpDGHTFMQAGFRKAIQQI--ESFNSGNK 76
Cdd:cd01472    25 VKRVVERLdIGPDgVRVGVVQYSDDPRTEFYLNtyRSKDDVLEAVKNLRYI--GGGTNTGKALKYVRENLftEASGSREG 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217275794  77 VPSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADYNLDQITAIADSPG--HVFAVEN 139
Cdd:cd01472   103 VPKVLVVITDGKS-----QDDVEEpAVELKQAGIEVFAVGVKNADEEELKQIASDPKelYVFNVAD 163
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 3-139 1.69e-05

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: 45.36  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   3 VEETVARFQ-SPN-IRMCFITYSTDGQTVLPLTSDKNRiKNGLDQLQKI-VPDGHTFMQAGFRKAIQQIESFNSG--NKV 77
Cdd:cd01482    25 LSSVVEAFEiGPDgVQVGLVQYSDDPRTEFDLNAYTSK-EDVLAAIKNLpYKGGNTRTGKALTHVREKNFTPDAGarPGV 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217275794  78 PSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADYNLDQITAIADSPG--HVFAVEN 139
Cdd:cd01482   104 PKVVILITDGKS-----QDDVELpARVLRNLGVNVFAVGVKDADESELKMIASKPSetHVFNVAD 163
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 77-179 2.60e-05

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: 45.45  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794  77 VPSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADYNLDQITAIADSP--GHVFAVENgFkalrSTIDALTS 153
Cdd:cd01475   108 VPRVGIVVTDGRP-----QDDVSEvAAKARALGIEMFAVGVGRADEEELREIASEPlaDHVFYVED-F----STIEELTK 177

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217275794 154 K----VCLDvtsvepSSECVGEPyHVVIHG 179
Cdd:cd01475   178 KfqgkICVV------PDLCATLS-HVCQQV 200
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 3-141 3.36e-04

VWA BatA 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. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 41.55  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275794   3 VEETVARF--QSPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPDGHTFMQAGFRKAIQQIESFNSGNKVpsm 80
Cdd:cd01467    29 AKEVLSDFidRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGLAGQGTAIGDAIGLAIKRLKNSEAKERV--- 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217275794  81 IIAMTDGELVAhAFQDTLREAQKARKLGANVYTLGVADY------------NLDQITAIAD-SPGHVFAVENGF 141
Cdd:cd01467   106 IVLLTDGENNA-GEIDPATAAELAKNKGVRIYTIGVGKSgsgpkpdgstilDEDSLVEIADkTGGRIFRALDGF 178
VWA_2 pfam13519
von Willebrand factor type A domain;
11-82 9.00e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 36.12  E-value: 9.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217275794  11 QSPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQkiVPDGHTFMQAGFRKAIQQIesFNSGNKVPSMII 82
Cdd:pfam13519  34 SLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLE--PKGGGTNLAAALQLARAAL--KHRRKNQPRRIV 101
 
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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