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Conserved domains on  [gi|767961955|ref|XP_011537735|]
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anthrax toxin receptor-like isoform X6 [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
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 138-237 7.28e-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: 158.57  E-value: 7.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955  138 KVCLDVTSVEPSSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 217
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|
gi 767961955  218 SLNKGKTFFKSNVSITSTTC 237
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTC 100
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1-143 2.42e-42

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: 149.20  E-value: 2.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   1 MCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPDGHTFMQAGFRKAIQQIESFN-SGNKVPSMIIAMTDGELVAHAFQ 79
Cdd:cd01474   42 FSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENANEQIFNRNgGGRETVSVIIALTDGQLLLNGHK 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961955  80 DTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHVFAVENGFKALRSTIDALTSKVCLDV 143
Cdd:cd01474  122 YPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFPVTSGFQALSGIIESVVKKACIEI 185
 
Name Accession Description Interval E-value
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 138-237 7.28e-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: 158.57  E-value: 7.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955  138 KVCLDVTSVEPSSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 217
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|
gi 767961955  218 SLNKGKTFFKSNVSITSTTC 237
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTC 100
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1-143 2.42e-42

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: 149.20  E-value: 2.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   1 MCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPDGHTFMQAGFRKAIQQIESFN-SGNKVPSMIIAMTDGELVAHAFQ 79
Cdd:cd01474   42 FSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENANEQIFNRNgGGRETVSVIIALTDGQLLLNGHK 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961955  80 DTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHVFAVENGFKALRSTIDALTSKVCLDV 143
Cdd:cd01474  122 YPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFPVTSGFQALSGIIESVVKKACIEI 185
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-135 1.96e-14

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: 73.43  E-value: 1.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   4 ITYSTDGQTVLPLTSDKNRIKNGLDQLQkivPDGHTFMQAGFRKAIQQIESFNSGNKVpsMIIAMTDGElvAHA-FQDTL 82
Cdd:COG1240  134 VAFGGEAEVLLPLTRDREALKRALDELP---PGGGTPLGDALALALELLKRADPARRK--VIVLLTDGR--DNAgRIDPL 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767961955  83 REAQKARKLGANVYTLGVAD--YNLDQITAIAD-SPGHVFAVENgFKALRSTIDAL 135
Cdd:COG1240  207 EAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEaTGGRYFRADD-LSELAAIYREI 261
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 4-123 1.99e-13

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: 68.64  E-value: 1.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955     4 ITYSTDGQTVLPL--TSDKNRIKNGLDQLQKiVPDGHTFMQAGFRKAIQQIESFNSGNK--VPSMIIAMTDGELVAHAfQ 79
Cdd:smart00327  43 VTFSDDARVLFPLndSRSKDALLEALASLSY-KLGGGTNLGAALQYALENLFSKSAGSRrgAPKVVILITDGESNDGP-K 120

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 767961955    80 DTLREAQKARKLGANVYTLGV-ADYNLDQITAIADSPGHVFAVEN 123
Cdd:smart00327 121 DLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGGVYVFLP 165
VWA pfam00092
von Willebrand factor type A domain;
3-134 1.19e-12

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 66.14  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955    3 FITYSTDGQTVLPLTSDKNR--IKNGLDQLqKIVPDGHTFMQAGFRKAIQQI--ESFNSGNKVPSMIIAMTDGElvaHAF 78
Cdd:pfam00092  42 LVQYSSDVRTEFPLNDYSSKeeLLSAVDNL-RYLGGGTTNTGKALKYALENLfsSAAGARPGAPKVVVLLTDGR---SQD 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767961955   79 QDTLREAQKARKLGANVYTLGVADYNLDQITAIADSP--GHVFAVENgFKALRSTIDA 134
Cdd:pfam00092 118 GDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGHVFTVSD-FEALEDLQDQ 174
 
Name Accession Description Interval E-value
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 138-237 7.28e-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: 158.57  E-value: 7.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955  138 KVCLDVTSVEPSSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 217
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|
gi 767961955  218 SLNKGKTFFKSNVSITSTTC 237
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTC 100
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1-143 2.42e-42

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: 149.20  E-value: 2.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   1 MCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPDGHTFMQAGFRKAIQQIESFN-SGNKVPSMIIAMTDGELVAHAFQ 79
Cdd:cd01474   42 FSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENANEQIFNRNgGGRETVSVIIALTDGQLLLNGHK 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961955  80 DTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHVFAVENGFKALRSTIDALTSKVCLDV 143
Cdd:cd01474  122 YPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFPVTSGFQALSGIIESVVKKACIEI 185
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 3-119 8.25e-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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 77.72  E-value: 8.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   3 FITYSTDGQTVLPLTSDKNR--IKNGLDQLQKIVPDGhTFMQAGFRKAIQQI-ESFNSGNKVPSMIIAMTDGElvAHAFQ 79
Cdd:cd01450   43 LVQYSDDVRVEFSLNDYKSKddLLKAVKNLKYLGGGG-TNTGKALQYALEQLfSESNARENVPKVIIVLTDGR--SDDGG 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767961955  80 DTLREAQKARKLGANVYTLGVADYNLDQITAIADSPG--HVF 119
Cdd:cd01450  120 DPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSerHVF 161
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-135 1.96e-14

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: 73.43  E-value: 1.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   4 ITYSTDGQTVLPLTSDKNRIKNGLDQLQkivPDGHTFMQAGFRKAIQQIESFNSGNKVpsMIIAMTDGElvAHA-FQDTL 82
Cdd:COG1240  134 VAFGGEAEVLLPLTRDREALKRALDELP---PGGGTPLGDALALALELLKRADPARRK--VIVLLTDGR--DNAgRIDPL 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767961955  83 REAQKARKLGANVYTLGVAD--YNLDQITAIAD-SPGHVFAVENgFKALRSTIDAL 135
Cdd:COG1240  207 EAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEaTGGRYFRADD-LSELAAIYREI 261
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 3-119 1.51e-13

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: 68.36  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   3 FITYSTDGQTVLPLT--SDKNRIKNGLDQLQKIvPDGHTFMQAGFRKAIQQIESFNSGNkVPSMIIAMTDGElVAHAFQD 80
Cdd:cd00198   43 LVTFGSNARVVLPLTtdTDKADLLEAIDALKKG-LGGGTNIGAALRLALELLKSAKRPN-ARRVIILLTDGE-PNDGPEL 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767961955  81 TLREAQKARKLGANVYTLGV-ADYNLDQITAIAD--SPGHVF 119
Cdd:cd00198  120 LAEAARELRKLGITVYTIGIgDDANEDELKEIADktTGGAVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 4-123 1.99e-13

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: 68.64  E-value: 1.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955     4 ITYSTDGQTVLPL--TSDKNRIKNGLDQLQKiVPDGHTFMQAGFRKAIQQIESFNSGNK--VPSMIIAMTDGELVAHAfQ 79
Cdd:smart00327  43 VTFSDDARVLFPLndSRSKDALLEALASLSY-KLGGGTNLGAALQYALENLFSKSAGSRrgAPKVVILITDGESNDGP-K 120

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 767961955    80 DTLREAQKARKLGANVYTLGV-ADYNLDQITAIADSPGHVFAVEN 123
Cdd:smart00327 121 DLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGGVYVFLP 165
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 4-113 2.63e-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: 70.52  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   4 ITYSTDGQTVLPLTS--DKNRIKNGLDQLQkivPDGHTFMQAGFRKAIQQIESFNSGNKVPSMIIaMTDGELVAHA--FQ 79
Cdd:COG2304  132 VTFAGDARVLLPPTPatDRAKILAAIDRLQ---AGGGTALGAGLELAYELARKHFIPGRVNRVIL-LTDGDANVGItdPE 207

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767961955  80 DTLREAQKARKLGANVYTLGV-ADYNLDQITAIAD 113
Cdd:COG2304  208 ELLKLAEEAREEGITLTTLGVgSDYNEDLLERLAD 242
VWA pfam00092
von Willebrand factor type A domain;
3-134 1.19e-12

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 66.14  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955    3 FITYSTDGQTVLPLTSDKNR--IKNGLDQLqKIVPDGHTFMQAGFRKAIQQI--ESFNSGNKVPSMIIAMTDGElvaHAF 78
Cdd:pfam00092  42 LVQYSSDVRTEFPLNDYSSKeeLLSAVDNL-RYLGGGTTNTGKALKYALENLfsSAAGARPGAPKVVVLLTDGR---SQD 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767961955   79 QDTLREAQKARKLGANVYTLGVADYNLDQITAIADSP--GHVFAVENgFKALRSTIDA 134
Cdd:pfam00092 118 GDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGHVFTVSD-FEALEDLQDQ 174
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 4-121 5.24e-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: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   4 ITYSTDGQTVLPLTS--DKNRIKNGLDQLQkivPDGHTFMQAGFRKAIQQIESfNSGNKVPSMIIAMTDGEL-VAHAFQD 80
Cdd:cd01465   41 VTYDGAAETVLPATPvrDKAAILAAIDRLT---AGGSTAGGAGIQLGYQEAQK-HFVPGGVNRILLATDGDFnVGETDPD 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767961955  81 TLRE-AQKARKLGANVYTLGVAD-YNLDQITAIADSPGHVFAV 121
Cdd:cd01465  117 ELARlVAQKRESGITLSTLGFGDnYNEDLMEAIADAGNGNTAY 159
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 4-103 1.25e-07

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: 52.00  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   4 ITYSTDGQTVLPLTS----DKNRIKNGLDQLQKI-VPDGHTFMQAGFRKAIQQIESFNSG-NKVPSMIIAMTDGElvAHA 77
Cdd:cd01471   45 VTFSTNAKELIRLSSpnstNKDLALNAIRALLSLyYPNGSTNTTSALLVVEKHLFDTRGNrENAPQLVIIMTDGI--PDS 122

                         90       100
                 ....*....|....*....|....*.
gi 767961955  78 FQDTLREAQKARKLGANVYTLGVADY 103
Cdd:cd01471  123 KFRTLKEARKLRERGVIIAVLGVGQG 148
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 6-123 6.97e-06

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: 46.45  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955   6 YSTDGQTVLPLT--SDKNRIKNGLDQLQKIvpDGHTFMQAGFRKAIQQI--ESFNSGNKVPSMIIAMTDGELvahafQDT 81
Cdd:cd01472   46 YSDDPRTEFYLNtyRSKDDVLEAVKNLRYI--GGGTNTGKALKYVRENLftEASGSREGVPKVLVVITDGKS-----QDD 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767961955  82 LRE-AQKARKLGANVYTLGVADYNLDQITAIADSPG--HVFAVEN 123
Cdd:cd01472  119 VEEpAVELKQAGIEVFAVGVKNADEEELKQIASDPKelYVFNVAD 163
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 61-163 2.50e-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: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955  61 VPSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADYNLDQITAIADSP--GHVFAVENgFkalrSTIDALTS 137
Cdd:cd01475  108 VPRVGIVVTDGRP-----QDDVSEvAAKARALGIEMFAVGVGRADEEELREIASEPlaDHVFYVED-F----STIEELTK 177

                         90       100       110
                 ....*....|....*....|....*....|
gi 767961955 138 K----VCLDvtsvepSSECVGEPyHVVIHG 163
Cdd:cd01475  178 KfqgkICVV------PDLCATLS-HVCQQV 200
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 37-123 1.58e-04

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: 42.27  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961955  37 GHTFMQAGFRKAIQQIESFNSG--NKVPSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADYNLDQITAIAD 113
Cdd:cd01482   77 GNTRTGKALTHVREKNFTPDAGarPGVPKVVILITDGKS-----QDDVELpARVLRNLGVNVFAVGVKDADESELKMIAS 151

                         90
                 ....*....|..
gi 767961955 114 SPG--HVFAVEN 123
Cdd:cd01482  152 KPSetHVFNVAD 163
 
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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