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Conserved domains on  [gi|2462517373|ref|XP_054220953|]
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anthrax toxin receptor-like isoform X7 [Homo sapiens]

Protein Classification

vWA domain-containing protein( domain architecture ID 10208431)

vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, hemostasis, signaling, chromosomal stability, malignant transformation, and immune defenses

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 ...
 98-197 4.33e-46

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: 155.49  E-value: 4.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373  98 KVCLDVTSVEASSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 177
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|
gi 2462517373 178 SLNKGKTFFKSNVSITSTTC 197
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTC 100
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1-103 5.29e-26

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: 104.51  E-value: 5.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373   1 MQAGFRKAIQQIESFN-SGNKVPSMIIAMTDGELVAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHVF 79
Cdd:cd01474    82 IHEGLENANEQIFNRNgGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVF 161

                          90       100
                  ....*....|....*....|....
gi 2462517373  80 AVENGFKALRSTIDALTSKVCLDV 103
Cdd:cd01474   162 PVTSGFQALSGIIESVVKKACIEI 185
 
Name Accession Description Interval E-value
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 98-197 4.33e-46

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: 155.49  E-value: 4.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373  98 KVCLDVTSVEASSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 177
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|
gi 2462517373 178 SLNKGKTFFKSNVSITSTTC 197
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTC 100
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1-103 5.29e-26

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: 104.51  E-value: 5.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373   1 MQAGFRKAIQQIESFN-SGNKVPSMIIAMTDGELVAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHVF 79
Cdd:cd01474    82 IHEGLENANEQIFNRNgGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVF 161

                          90       100
                  ....*....|....*....|....
gi 2462517373  80 AVENGFKALRSTIDALTSKVCLDV 103
Cdd:cd01474   162 PVTSGFQALSGIIESVVKKACIEI 185
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1-83 1.59e-07

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: 51.30  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373    1 MQAGFRKAIQQIESFNSGNK--VPSMIIAMTDGELVAHAfQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIADSPGH 77
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRrgAPKVVILITDGESNDGP-KDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159


                   ....*.
gi 2462517373   78 VFAVEN 83
Cdd:smart00327 160 VYVFLP 165
VWA pfam00092
von Willebrand factor type A domain;
3-94 2.49e-07

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 50.74  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373   3 AGFRKAIQQI--ESFNSGNKVPSMIIAMTDGElvaHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSP--GHV 78
Cdd:pfam00092  83 KALKYALENLfsSAAGARPGAPKVVVLLTDGR---SQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGHV 159

                          90
                  ....*....|....*.
gi 2462517373  79 FAVENgFKALRSTIDA 94
Cdd:pfam00092 160 FTVSD-FEALEDLQDQ 174
 
Name Accession Description Interval E-value
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 98-197 4.33e-46

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: 155.49  E-value: 4.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373  98 KVCLDVTSVEASSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 177
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|
gi 2462517373 178 SLNKGKTFFKSNVSITSTTC 197
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTC 100
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 1-103 5.29e-26

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: 104.51  E-value: 5.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373   1 MQAGFRKAIQQIESFN-SGNKVPSMIIAMTDGELVAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHVF 79
Cdd:cd01474    82 IHEGLENANEQIFNRNgGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVF 161

                          90       100
                  ....*....|....*....|....
gi 2462517373  80 AVENGFKALRSTIDALTSKVCLDV 103
Cdd:cd01474   162 PVTSGFQALSGIIESVVKKACIEI 185
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1-79 3.58e-08

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: 52.68  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373   1 MQAGFRKAIQQI-ESFNSGNKVPSMIIAMTDGElvAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPG--H 77
Cdd:cd01450    82 TGKALQYALEQLfSESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSerH 159


                  ..
gi 2462517373  78 VF 79
Cdd:cd01450   160 VF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1-83 1.59e-07

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: 51.30  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373    1 MQAGFRKAIQQIESFNSGNK--VPSMIIAMTDGELVAHAfQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIADSPGH 77
Cdd:smart00327  81 LGAALQYALENLFSKSAGSRrgAPKVVILITDGESNDGP-KDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPGG 159


                   ....*.
gi 2462517373   78 VFAVEN 83
Cdd:smart00327 160 VYVFLP 165
VWA pfam00092
von Willebrand factor type A domain;
3-94 2.49e-07

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 50.74  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373   3 AGFRKAIQQI--ESFNSGNKVPSMIIAMTDGElvaHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSP--GHV 78
Cdd:pfam00092  83 KALKYALENLfsSAAGARPGAPKVVVLLTDGR---SQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPgeGHV 159

                          90
                  ....*....|....*.
gi 2462517373  79 FAVENgFKALRSTIDA 94
Cdd:pfam00092 160 FTVSD-FEALEDLQDQ 174
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 3-79 2.85e-06

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: 47.18  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373   3 AGFRKAIQQIESFNSGNkVPSMIIAMTDGElVAHAFQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIAD--SPGHVF 79
Cdd:cd00198    84 AALRLALELLKSAKRPN-ARRVIILLTDGE-PNDGPELLAEAARELRKLGITVYTIGIgDDANEDELKEIADktTGGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 21-123 1.22e-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: 46.22  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517373  21 VPSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADYNLDQITAIADSP--GHVFAVENgFkalrSTIDALTS 97
Cdd:cd01475   108 VPRVGIVVTDGRP-----QDDVSEvAAKARALGIEMFAVGVGRADEEELREIASEPlaDHVFYVED-F----STIEELTK 177

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462517373  98 K----VCldvtsvEASSECVGEPyHVVIHG 123
Cdd:cd01475   178 KfqgkIC------VVPDLCATLS-HVCQQV 200
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 20-83 1.52e-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: 1.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462517373  20 KVPSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADYNLDQITAIADSPG--HVFAVEN 83
Cdd:cd01482   102 GVPKVVILITDGKS-----QDDVELpARVLRNLGVNVFAVGVKDADESELKMIASKPSetHVFNVAD 163
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 12-83 5.56e-04

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: 40.67  E-value: 5.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462517373  12 IESFNSGNKVPSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADYNLDQITAIADSPG--HVFAVEN 83
Cdd:cd01472    94 TEASGSREGVPKVLVVITDGKS-----QDDVEEpAVELKQAGIEVFAVGVKNADEEELKQIASDPKelYVFNVAD 163
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 19-63 9.93e-04

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: 40.06  E-value: 9.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462517373  19 NKVPSMIIAMTDGElvAHAFQDTLREAQKARKLGANVYTLGVADY 63
Cdd:cd01471   106 ENAPQLVIIMTDGI--PDSKFRTLKEARKLRERGVIIAVLGVGQG 148
 
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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