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Conserved domains on  [gi|2024509993|ref|XP_040531196|]
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anthrax toxin receptor-like [Gallus gallus]

Protein Classification

anthrax toxin receptor( domain architecture ID 10107125)

anthrax toxin receptor is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells

CATH:  3.40.50.410
Gene Ontology:  GO:0004888|GO:0046872
PubMed:  12579041|10830113|12388743
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 42-226 1.03e-95

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: 289.41  E-value: 1.03e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  42 CHGAFDLYFILDKSGSVRNHWTEIYSFVESLAEKFISPMLRMSFIVFSSRGTTIMKLTENREAIRRGLEILQYEVPGGDT 121
Cdd:cd01474     1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 122 FMHEGFKRANEQIYHETYGGVRTASVIIALTDGELQDVQFYYAEQEANRARSFGAIVYCVGVKDFNETQLSTIADSIDHV 201
Cdd:cd01474    81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                         170       180
                  ....*....|....*....|....*
gi 2024509993 202 FPVTGGFYALRGTIDSILKKSCIEI 226
Cdd:cd01474   161 FPVTSGFQALSGIIESVVKKACIEI 185
Ant_C pfam05586
Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic ...
 399-491 5.34e-67

Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic C-terminus of the anthrax receptor.


:

Pssm-ID: 461683  Cd Length: 93  Bit Score: 211.78  E-value: 5.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 399 VRWGDKGSTEEGAKLEKPKNAIIKLPEQEYEPWEPKPKKPHVRKPPSQRKWYTPIKGKLDALWALVRRGYDQVSLMRPQP 478
Cdd:pfam05586   1 VRWGEKGSTEEGAKLEKAKNAVVKMPEEEEEPPEPRPRKPPARKPPPQRKWYTPIKGKLDALWALLRRGYDRVSLMRPTP 80

                          90
                  ....*....|...
gi 2024509993 479 GDKGRCINFTRVK 491
Cdd:pfam05586  81 GDKGRCINFTRVK 93
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 221-308 1.07e-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: 158.57  E-value: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 221 KSCIEILAAEPSSVCAGEPFQVVVRGNGFYHARNIDQVLCSFKLNDSLTINEKPTLVHDTYLLCPAPVIEDAGQVVFLQV 300
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80


                  ....*...
gi 2024509993 301 SMNNGLTF 308
Cdd:pfam05587  81 SLNNGKSF 88
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 42-226 1.03e-95

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: 289.41  E-value: 1.03e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  42 CHGAFDLYFILDKSGSVRNHWTEIYSFVESLAEKFISPMLRMSFIVFSSRGTTIMKLTENREAIRRGLEILQYEVPGGDT 121
Cdd:cd01474     1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 122 FMHEGFKRANEQIYHETYGGVRTASVIIALTDGELQDVQFYYAEQEANRARSFGAIVYCVGVKDFNETQLSTIADSIDHV 201
Cdd:cd01474    81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                         170       180
                  ....*....|....*....|....*
gi 2024509993 202 FPVTGGFYALRGTIDSILKKSCIEI 226
Cdd:cd01474   161 FPVTSGFQALSGIIESVVKKACIEI 185
Ant_C pfam05586
Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic ...
 399-491 5.34e-67

Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic C-terminus of the anthrax receptor.


Pssm-ID: 461683  Cd Length: 93  Bit Score: 211.78  E-value: 5.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 399 VRWGDKGSTEEGAKLEKPKNAIIKLPEQEYEPWEPKPKKPHVRKPPSQRKWYTPIKGKLDALWALVRRGYDQVSLMRPQP 478
Cdd:pfam05586   1 VRWGEKGSTEEGAKLEKAKNAVVKMPEEEEEPPEPRPRKPPARKPPPQRKWYTPIKGKLDALWALLRRGYDRVSLMRPTP 80

                          90
                  ....*....|...
gi 2024509993 479 GDKGRCINFTRVK 491
Cdd:pfam05586  81 GDKGRCINFTRVK 93
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 221-308 1.07e-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: 158.57  E-value: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 221 KSCIEILAAEPSSVCAGEPFQVVVRGNGFYHARNIDQVLCSFKLNDSLTINEKPTLVHDTYLLCPAPVIEDAGQVVFLQV 300
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80


                  ....*...
gi 2024509993 301 SMNNGLTF 308
Cdd:pfam05587  81 SLNNGKSF 88
VWA pfam00092
von Willebrand factor type A domain;
47-202 5.05e-23

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.19  E-value: 5.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGSVRNH-WTEIYSFVESLAEKF-ISPML-RMSFIVFSSRGTTIMKLTE--NREAIRRGLEILQYEvPGGDT 121
Cdd:pfam00092   1 DIVFLLDGSGSIGGDnFEKVKEFLKKLVESLdIGPDGtRVGLVQYSSDVRTEFPLNDysSKEELLSAVDNLRYL-GGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 122 FMHEGFKRANEQIYHETYGGVRTAS-VIIALTDGELQDvqfYYAEQEANRARSFGAIVYCVGVKDFNETQLSTIA--DSI 198
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGARPGAPkVVVLLTDGRSQD---GDPEEVARELKSAGVTVFAVGVGNADDEELRKIAsePGE 156


                  ....
gi 2024509993 199 DHVF 202
Cdd:pfam00092 157 GHVF 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 47-220 1.64e-20

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: 89.05  E-value: 1.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993   47 DLYFILDKSGSVR-NHWTEIYSFVESLAEKF-ISPML-RMSFIVFSSRGTTIMKL--TENREAIRRGLEILQYEvPGGDT 121
Cdd:smart00327   1 DVVFLLDGSGSMGgNRFELAKEFVLKLVEQLdIGPDGdRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYK-LGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  122 FMHEGFKRANEQIYHETYGGVRTA-SVIIALTDGELQDVQFYYAEqEANRARSFGAIVYCVGVK-DFNETQLSTIADsid 199
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGApKVVILITDGESNDGPKDLLK-AAKELKRSGVKVFVVGVGnDVDEEELKKLAS--- 155

                          170       180
                   ....*....|....*....|.
gi 2024509993  200 hvfPVTGGFYALRGTIDSILK 220
Cdd:smart00327 156 ---APGGVYVFLPELLDLLID 173
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 47-209 2.37e-13

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: 70.35  E-value: 2.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGS--VRNHWTEIYSFVESLAEKFISPMlRMSFIVFSSRGTTIMKLTENREAIRRGLEILQyevPGGDTFMH 124
Cdd:COG1240    94 DVVLVVDASGSmaAENRLEAAKGALLDFLDDYRPRD-RVGLVAFGGEAEVLLPLTRDREALKRALDELP---PGGGTPLG 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 125 EGFKRANEQIYHETYGGVRtasVIIALTDGElQDVQFYYAEQEANRARSFGAIVYCVGVKD--FNETQLSTIADSidhvf 202
Cdd:COG1240   170 DALALALELLKRADPARRK---VIVLLTDGR-DNAGRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEA----- 240


                  ....*..
gi 2024509993 203 pvTGGFY 209
Cdd:COG1240   241 --TGGRY 245
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 402-523 1.50e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.68  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 402 GDKGSTEEGAKLEKPKnaiiklPEQEYEPWE-------PK-PKKP-HVRKPPSQRKWYTPIKGKLDalwalVRRGydqvS 472
Cdd:PTZ00449  547 GKPGETKEGEVGKKPG------PAKEHKPSKiptlskkPEfPKDPkHPKDPEEPKKPKRPRSAQRP-----TRPK----S 611

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024509993 473 LMRPQPGDkgrcINFTRVKSDGTSAPYSPP----PKLPRRDNVNHAPRSPSPPAS 523
Cdd:PTZ00449  612 PKLPELLD----IPKSPKRPESPKSPKRPPppqrPSSPERPEGPKIIKSPKPPKS 662
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 42-226 1.03e-95

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: 289.41  E-value: 1.03e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  42 CHGAFDLYFILDKSGSVRNHWTEIYSFVESLAEKFISPMLRMSFIVFSSRGTTIMKLTENREAIRRGLEILQYEVPGGDT 121
Cdd:cd01474     1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 122 FMHEGFKRANEQIYHETYGGVRTASVIIALTDGELQDVQFYYAEQEANRARSFGAIVYCVGVKDFNETQLSTIADSIDHV 201
Cdd:cd01474    81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                         170       180
                  ....*....|....*....|....*
gi 2024509993 202 FPVTGGFYALRGTIDSILKKSCIEI 226
Cdd:cd01474   161 FPVTSGFQALSGIIESVVKKACIEI 185
Ant_C pfam05586
Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic ...
 399-491 5.34e-67

Anthrax receptor C-terminus region; This region is found in the putatively cytoplasmic C-terminus of the anthrax receptor.


Pssm-ID: 461683  Cd Length: 93  Bit Score: 211.78  E-value: 5.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 399 VRWGDKGSTEEGAKLEKPKNAIIKLPEQEYEPWEPKPKKPHVRKPPSQRKWYTPIKGKLDALWALVRRGYDQVSLMRPQP 478
Cdd:pfam05586   1 VRWGEKGSTEEGAKLEKAKNAVVKMPEEEEEPPEPRPRKPPARKPPPQRKWYTPIKGKLDALWALLRRGYDRVSLMRPTP 80

                          90
                  ....*....|...
gi 2024509993 479 GDKGRCINFTRVK 491
Cdd:pfam05586  81 GDKGRCINFTRVK 93
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 221-308 1.07e-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: 158.57  E-value: 1.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 221 KSCIEILAAEPSSVCAGEPFQVVVRGNGFYHARNIDQVLCSFKLNDSLTINEKPTLVHDTYLLCPAPVIEDAGQVVFLQV 300
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80


                  ....*...
gi 2024509993 301 SMNNGLTF 308
Cdd:pfam05587  81 SLNNGKSF 88
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 46-202 3.91e-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: 112.77  E-value: 3.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  46 FDLYFILDKSGSVRNHW-TEIYSFVESLAEKF-ISPML-RMSFIVFSSRGTTIMKLTE--NREAIRRGLEILQYEVpGGD 120
Cdd:cd01450     1 LDIVFLLDGSESVGPENfEKVKDFIEKLVEKLdIGPDKtRVGLVQYSDDVRVEFSLNDykSKDDLLKAVKNLKYLG-GGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 121 TFMHEGFKRANEQIYHETYGGVRTASVIIALTDGELQDvqFYYAEQEANRARSFGAIVYCVGVKDFNETQLSTIAD--SI 198
Cdd:cd01450    80 TNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDD--GGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIAScpSE 157


                  ....
gi 2024509993 199 DHVF 202
Cdd:cd01450   158 RHVF 161
VWA pfam00092
von Willebrand factor type A domain;
47-202 5.05e-23

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 96.19  E-value: 5.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGSVRNH-WTEIYSFVESLAEKF-ISPML-RMSFIVFSSRGTTIMKLTE--NREAIRRGLEILQYEvPGGDT 121
Cdd:pfam00092   1 DIVFLLDGSGSIGGDnFEKVKEFLKKLVESLdIGPDGtRVGLVQYSSDVRTEFPLNDysSKEELLSAVDNLRYL-GGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 122 FMHEGFKRANEQIYHETYGGVRTAS-VIIALTDGELQDvqfYYAEQEANRARSFGAIVYCVGVKDFNETQLSTIA--DSI 198
Cdd:pfam00092  80 NTGKALKYALENLFSSAAGARPGAPkVVVLLTDGRSQD---GDPEEVARELKSAGVTVFAVGVGNADDEELRKIAsePGE 156


                  ....
gi 2024509993 199 DHVF 202
Cdd:pfam00092 157 GHVF 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 47-220 1.64e-20

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: 89.05  E-value: 1.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993   47 DLYFILDKSGSVR-NHWTEIYSFVESLAEKF-ISPML-RMSFIVFSSRGTTIMKL--TENREAIRRGLEILQYEvPGGDT 121
Cdd:smart00327   1 DVVFLLDGSGSMGgNRFELAKEFVLKLVEQLdIGPDGdRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYK-LGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  122 FMHEGFKRANEQIYHETYGGVRTA-SVIIALTDGELQDVQFYYAEqEANRARSFGAIVYCVGVK-DFNETQLSTIADsid 199
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGApKVVILITDGESNDGPKDLLK-AAKELKRSGVKVFVVGVGnDVDEEELKKLAS--- 155

                          170       180
                   ....*....|....*....|.
gi 2024509993  200 hvfPVTGGFYALRGTIDSILK 220
Cdd:smart00327 156 ---APGGVYVFLPELLDLLID 173
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 47-196 8.34e-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: 77.99  E-value: 8.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGSV-RNHWTEIYSFVESLAEKFISPML--RMSFIVFSSRGTTIMKLTE--NREAIRRGLEILQYEvPGGDT 121
Cdd:cd00198     2 DIVFLLDVSGSMgGEKLDKAKEALKALVSSLSASPPgdRVGLVTFGSNARVVLPLTTdtDKADLLEAIDALKKG-LGGGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024509993 122 FMHEGFKRANEQIYHETYGGVRtaSVIIALTDGELQDVQFYYAEqEANRARSFGAIVYCVGVKD-FNETQLSTIAD 196
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNAR--RVIILLTDGEPNDGPELLAE-AARELRKLGITVYTIGIGDdANEDELKEIAD 153
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 47-205 1.83e-14

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: 71.11  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGSV-RNHWTEIYSFVESLAEKF-ISPML-RMSFIVFSSRGTTIMKLTE--NREAIRRGLEILQYEvpGGDT 121
Cdd:cd01472     2 DIVFLVDGSESIgLSNFNLVKDFVKRVVERLdIGPDGvRVGVVQYSDDPRTEFYLNTyrSKDDVLEAVKNLRYI--GGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 122 FMHEGFKRANEQIYHETYG---GVRtaSVIIALTDGELQDVqfyyAEQEANRARSFGAIVYCVGVKDFNETQLSTIA--D 196
Cdd:cd01472    80 NTGKALKYVRENLFTEASGsreGVP--KVLVVITDGKSQDD----VEEPAVELKQAGIEVFAVGVKNADEEELKQIAsdP 153


                  ....*....
gi 2024509993 197 SIDHVFPVT 205
Cdd:cd01472   154 KELYVFNVA 162
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 47-209 2.37e-13

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: 70.35  E-value: 2.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGS--VRNHWTEIYSFVESLAEKFISPMlRMSFIVFSSRGTTIMKLTENREAIRRGLEILQyevPGGDTFMH 124
Cdd:COG1240    94 DVVLVVDASGSmaAENRLEAAKGALLDFLDDYRPRD-RVGLVAFGGEAEVLLPLTRDREALKRALDELP---PGGGTPLG 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 125 EGFKRANEQIYHETYGGVRtasVIIALTDGElQDVQFYYAEQEANRARSFGAIVYCVGVKD--FNETQLSTIADSidhvf 202
Cdd:COG1240   170 DALALALELLKRADPARRK---VIVLLTDGR-DNAGRIDPLEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEA----- 240


                  ....*..
gi 2024509993 203 pvTGGFY 209
Cdd:COG1240   241 --TGGRY 245
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 47-204 4.06e-12

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: 64.62  E-value: 4.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGSV-RNHWTEIYSFVESLAEKF-ISPM-LRMSFIVFSSRGTTIMKLTE--NREAIRRGLEILQYEvpGGDT 121
Cdd:cd01482     2 DIVFLVDGSWSIgRSNFNLVRSFLSSVVEAFeIGPDgVQVGLVQYSDDPRTEFDLNAytSKEDVLAAIKNLPYK--GGNT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 122 FMHEGFKRANEQIYHETyGGVRT--ASVIIALTDGELQDVqfyyAEQEANRARSFGAIVYCVGVKDFNETQLSTIAD--S 197
Cdd:cd01482    80 RTGKALTHVREKNFTPD-AGARPgvPKVVILITDGKSQDD----VELPARVLRNLGVNVFAVGVKDADESELKMIASkpS 154


                  ....*..
gi 2024509993 198 IDHVFPV 204
Cdd:cd01482   155 ETHVFNV 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 47-202 8.40e-12

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: 63.57  E-value: 8.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGSVRNHWTEIYSFVESLAEKF-ISP-MLRMSFIVFSSRGTTIM--KLTE--NREAIRRGLEILQYEvpGGD 120
Cdd:cd01476     2 DLLFVLDSSGSVRGKFEKYKKYIERIVEGLeIGPtATRVALITYSGRGRQRVrfNLPKhnDGEELLEKVDNLRFI--GGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 121 TFMHEGFKRANEQIYHETYGGVRTASVIIALTDGELQDvqfyYAEQEANRARS-FGAIVYCVGVKD---FNETQLSTIAD 196
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRREGIPKVVVVLTDGRSHD----DPEKQARILRAvPNIETFAVGTGDpgtVDTEELHSITG 155


                  ....*.
gi 2024509993 197 SIDHVF 202
Cdd:cd01476   156 NEDHIF 161
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 47-183 6.30e-11

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: 61.63  E-value: 6.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGSVR--NHWTEIYSFVESLAEKF-ISP-MLRMSFIVFSSRGTTIMKLTEN--------REAIRRGLEIlqY 114
Cdd:cd01471     2 DLYLLVDGSGSIGysNWVTHVVPFLHTFVQNLnISPdEINLYLVTFSTNAKELIRLSSPnstnkdlaLNAIRALLSL--Y 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 115 EvPGGDTFMHEGFKRAnEQIYHETYGGVRTA-SVIIALTDGELQDVqfYYAEQEANRARSFGAIVYCVGV 183
Cdd:cd01471    80 Y-PNGSTNTTSALLVV-EKHLFDTRGNRENApQLVIIMTDGIPDSK--FRTLKEARKLRERGVIIAVLGV 145
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 44-195 2.76e-10

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: 59.71  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  44 GAFDLYFILDKSGSVRNHWTEIY-SFVESLAEKFISPML--------RMSFIVFSSRGTTI---MKLTENREAIRRGLEI 111
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITkNFVKRVAERFLKDYYrkdpagswRVGVVQYSDQQEVEagfLRDIRNYTSLKEAVDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 112 LQYEvpGGDTFMHEGFKRANEQIYHETYGGVRTASVIIalTDGELQDVQFYYAEQEANRARSFGAIVYCVGVKDFNETQL 191
Cdd:cd01480    81 LEYI--GGGTFTDCALKYATEQLLEGSHQKENKFLLVI--TDGHSDGSPDGGIEKAVNEADHLGIKIFFVAVGSQNEEPL 156


                  ....
gi 2024509993 192 STIA 195
Cdd:cd01480   157 SRIA 160
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 47-213 5.31e-08

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: 52.74  E-value: 5.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGSVR-NHWTEIYSFVESLAEKF-ISPM-LRMSFIVFSSRGTTIMKLTE--NREAIRRGLE-ILQYevpGGD 120
Cdd:cd01469     2 DIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLdIGPTkTQFGLVQYSESFRTEFTLNEyrTKEEPLSLVKhISQL---LGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 121 TFMHEGFKRANEQIYHETYGGVRTAS-VIIALTDGELQDVqfYYAEQEANRARSFGAIVYCVGVKDF--NET---QLSTI 194
Cdd:cd01469    79 TNTATAIQYVVTELFSESNGARKDATkVLVVITDGESHDD--PLLKDVIPQAEREGIIRYAIGVGGHfqRENsreELKTI 156

                         170       180
                  ....*....|....*....|.
gi 2024509993 195 AD--SIDHVFPVTgGFYALRG 213
Cdd:cd01469   157 ASkpPEEHFFNVT-DFAALKD 176
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 47-196 2.15e-07

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 52.37  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  47 DLYFILDKSGS---VRNHWT--EIYSFVESLAEKfispmLRMSFIVFSSRGTTIMKLTENREaIRRGLEILQYEVPGGDT 121
Cdd:COG2425   120 PVVLCVDTSGSmagSKEAAAkaAALALLRALRPN-----RRFGVILFDTEVVEDLPLTADDG-LEDAIEFLSGLFAGGGT 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024509993 122 FMHEGFKRANEQIYHETYggvRTASVIIaLTDGELQDVQFYYAeQEANRARSfGAIVYCVGVKDFNETQL-STIAD 196
Cdd:COG2425   194 DIAPALRAALELLEEPDY---RNADIVL-ITDGEAGVSPEELL-REVRAKES-GVRLFTVAIGDAGNPGLlEALAD 263
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 44-253 8.64e-07

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: 50.08  E-value: 8.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  44 GAFDLYFILDKSGSVRNhwteiYSFveSLAEKFISPML----------RMSFIVFSSRGTTIMKLT--ENREAIRRGLEI 111
Cdd:cd01475     1 GPTDLVFLIDSSRSVRP-----ENF--ELVKQFLNQIIdsldvgpdatRVGLVQYSSTVKQEFPLGrfKSKADLKRAVRR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 112 LQYEVPGgdTFMHEGFKRANEQIYHETYGG----VRTASVIIALTDGELQDvqfyYAEQEANRARSFGAIVYCVGVKDFN 187
Cdd:cd01475    74 MEYLETG--TMTGLAIQYAMNNAFSEAEGArpgsERVPRVGIVVTDGRPQD----DVSEVAAKARALGIEMFAVGVGRAD 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024509993 188 ETQLSTIAD--SIDHVFPVtggfyALRGTIDSILKKSCIEILAAepSSVCAGEP---FQVVVRGNGFYHAR 253
Cdd:cd01475   148 EEELREIASepLADHVFYV-----EDFSTIEELTKKFQGKICVV--PDLCATLShvcQQVCISTPGSYLCA 211
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
49-198 5.23e-05

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 44.53  E-value: 5.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  49 YFILDKSGSVR-------NhwTEIYSFVESL-AEKFISPMLRMSFIVFSSRGTTIMKLTEnreaiRRGLEILQYEVpGGD 120
Cdd:COG4245     9 YLLLDTSGSMSgepiealN--EGLQALIDELrQDPYALETVEVSVITFDGEAKVLLPLTD-----LEDFQPPDLSA-SGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 121 TFMHEGFKRA-----NEQIYHETYGGVRTASVIIALTDGELQDVQFyyaEQEANRARSF----GAIVYCVGVKDF-NETQ 190
Cdd:COG4245    81 TPLGAALELLldlieRRVQKYTAEGKGDWRPVVFLITDGEPTDSDW---EAALQRLKDGeaakKANIFAIGVGPDaDTEV 157


                  ....*...
gi 2024509993 191 LSTIADSI 198
Cdd:COG4245   158 LKQLTDPV 165
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 402-523 1.50e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 44.68  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993 402 GDKGSTEEGAKLEKPKnaiiklPEQEYEPWE-------PK-PKKP-HVRKPPSQRKWYTPIKGKLDalwalVRRGydqvS 472
Cdd:PTZ00449  547 GKPGETKEGEVGKKPG------PAKEHKPSKiptlskkPEfPKDPkHPKDPEEPKKPKRPRSAQRP-----TRPK----S 611

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024509993 473 LMRPQPGDkgrcINFTRVKSDGTSAPYSPP----PKLPRRDNVNHAPRSPSPPAS 523
Cdd:PTZ00449  612 PKLPELLD----IPKSPKRPESPKSPKRPPppqrPSSPERPEGPKIIKSPKPPKS 662
VWA_2 pfam13519
von Willebrand factor type A domain;
48-149 2.31e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 37.66  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509993  48 LYFILDKSGSVRN------HWTEIYSFVESLAEKFisPMLRMSFIVFSSRGTTIMKLTENREAIRRGLEILQYEvpGGDT 121
Cdd:pfam13519   1 LVFVLDTSGSMRNgdygptRLEAAKDAVLALLKSL--PGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLEPK--GGGT 76

                          90       100
                  ....*....|....*....|....*...
gi 2024509993 122 FMHEGFKRANEQIYHETYGgvRTASVII 149
Cdd:pfam13519  77 NLAAALQLARAALKHRRKN--QPRRIVL 102
 
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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