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Conserved domains on  [gi|767961975|ref|XP_011537743|]
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anthrax toxin receptor-like isoform X8 [Homo sapiens]

Protein Classification

vWFA and Anth_Ig domain-containing protein( domain architecture ID 10208431)

vWFA and Anth_Ig 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 ...
 71-254 1.03e-68

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: 215.07  E-value: 1.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  71 CQGSFDLYFILDKSGSVNNNWIDLYMWVEETVARFQSPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPDGHT 150
Cdd:cd01474    1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 151 FMQAGFRKAIQQIESFN-SGNKVPSMIIAMTDGELVAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHV 229
Cdd:cd01474   81 YIHEGLENANEQIFNRNgGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                        170       180
                 ....*....|....*....|....*
gi 767961975 230 FAVENGFKALRSTIDALTSKVCLDV 254
Cdd:cd01474  161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 249-349 1.30e-51

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: 167.81  E-value: 1.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  249 KVCLDVTSVEPSSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 328
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|.
gi 767961975  329 SLNKGKTFFKSNVSITSTTCV 349
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCS 101
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 71-254 1.03e-68

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: 215.07  E-value: 1.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  71 CQGSFDLYFILDKSGSVNNNWIDLYMWVEETVARFQSPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPDGHT 150
Cdd:cd01474    1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 151 FMQAGFRKAIQQIESFN-SGNKVPSMIIAMTDGELVAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHV 229
Cdd:cd01474   81 YIHEGLENANEQIFNRNgGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                        170       180
                 ....*....|....*....|....*
gi 767961975 230 FAVENGFKALRSTIDALTSKVCLDV 254
Cdd:cd01474  161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 249-349 1.30e-51

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: 167.81  E-value: 1.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  249 KVCLDVTSVEPSSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 328
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|.
gi 767961975  329 SLNKGKTFFKSNVSITSTTCV 349
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCS 101
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 76-234 3.39e-22

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: 92.52  E-value: 3.39e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975    76 DLYFILDKSGSVNNNWIDLYMW-VEETVARF--QSPNIRMCFITYSTDGQTVLPL--TSDKNRIKNGLDQLQKiVPDGHT 150
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEfVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSY-KLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975   151 FMQAGFRKAIQQIESFNSGNK--VPSMIIAMTDGELVAHAfQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIADSPG 227
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRrgAPKVVILITDGESNDGP-KDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPG 158


                   ....*..
gi 767961975   228 HVFAVEN 234
Cdd:smart00327 159 GVYVFLP 165
VWA pfam00092
von Willebrand factor type A domain;
76-245 3.76e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 84.25  E-value: 3.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975   76 DLYFILDKSGSVNN-NWIDLYMWVEETVARFQ--SPNIRMCFITYSTDGQTVLPLTSDKNR--IKNGLDQLqKIVPDGHT 150
Cdd:pfam00092   1 DIVFLLDGSGSIGGdNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKeeLLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  151 FMQAGFRKAIQQI--ESFNSGNKVPSMIIAMTDGElvaHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSP-- 226
Cdd:pfam00092  80 NTGKALKYALENLfsSAAGARPGAPKVVVLLTDGR---SQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPge 156

                         170
                  ....*....|....*....
gi 767961975  227 GHVFAVENgFKALRSTIDA 245
Cdd:pfam00092 157 GHVFTVSD-FEALEDLQDQ 174
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 66-246 4.17e-18

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: 83.45  E-value: 4.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  66 QAGHRCQGSFDLYFILDKSGSvnnnwidlyMWVE-------ETVARF---QSPNIRMCFITYSTDGQTVLPLTSDKNRIK 135
Cdd:COG1240   84 LALARPQRGRDVVLVVDASGS---------MAAEnrleaakGALLDFlddYRPRDRVGLVAFGGEAEVLLPLTRDREALK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 136 NGLDQLQkivPDGHTFMQAGFRKAIQQIESFNSGNKVpsMIIAMTDGElvAHA-FQDTLREAQKARKLGANVYTLGVAD- 213
Cdd:COG1240  155 RALDELP---PGGGTPLGDALALALELLKRADPARRK--VIVLLTDGR--DNAgRIDPLEAAELAAAAGIRIYTIGVGTe 227

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767961975 214 -YNLDQITAIAD-SPGHVFAVENgFKALRSTIDAL 246
Cdd:COG1240  228 aVDEGLLREIAEaTGGRYFRADD-LSELAAIYREI 261
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 71-254 1.03e-68

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: 215.07  E-value: 1.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  71 CQGSFDLYFILDKSGSVNNNWIDLYMWVEETVARFQSPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPDGHT 150
Cdd:cd01474    1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 151 FMQAGFRKAIQQIESFN-SGNKVPSMIIAMTDGELVAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPGHV 229
Cdd:cd01474   81 YIHEGLENANEQIFNRNgGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                        170       180
                 ....*....|....*....|....*
gi 767961975 230 FAVENGFKALRSTIDALTSKVCLDV 254
Cdd:cd01474  161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 249-349 1.30e-51

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: 167.81  E-value: 1.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  249 KVCLDVTSVEPSSECVGEPYHVVIHGNGFQNLKKRDEVICRFIFNESTIIDEKPTSIDNNSMNCPGPKLEKPGEEYSIEV 328
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|.
gi 767961975  329 SLNKGKTFFKSNVSITSTTCV 349
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCS 101
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 75-230 2.22e-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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 103.53  E-value: 2.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  75 FDLYFILDKSGSVNNNWIDLYM-WVEETVARF-QSPN-IRMCFITYSTDGQTVLPLTSDKNR--IKNGLDQLQKIVPDGh 149
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKdFIEKLVEKLdIGPDkTRVGLVQYSDDVRVEFSLNDYKSKddLLKAVKNLKYLGGGG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 150 TFMQAGFRKAIQQI-ESFNSGNKVPSMIIAMTDGElvAHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSPG- 227
Cdd:cd01450   80 TNTGKALQYALEQLfSESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPSe 157


                 ....
gi 767961975 228 -HVF 230
Cdd:cd01450  158 rHVF 161
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 76-234 3.39e-22

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: 92.52  E-value: 3.39e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975    76 DLYFILDKSGSVNNNWIDLYMW-VEETVARF--QSPNIRMCFITYSTDGQTVLPL--TSDKNRIKNGLDQLQKiVPDGHT 150
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEfVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSY-KLGGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975   151 FMQAGFRKAIQQIESFNSGNK--VPSMIIAMTDGELVAHAfQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIADSPG 227
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRrgAPKVVILITDGESNDGP-KDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLASAPG 158


                   ....*..
gi 767961975   228 HVFAVEN 234
Cdd:smart00327 159 GVYVFLP 165
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 76-230 3.74e-20

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: 86.47  E-value: 3.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  76 DLYFILDKSGSVNNNWIDLYMW-VEETVARFQ--SPNIRMCFITYSTDGQTVLPLT--SDKNRIKNGLDQLQKIvPDGHT 150
Cdd:cd00198    2 DIVFLLDVSGSMGGEKLDKAKEaLKALVSSLSasPPGDRVGLVTFGSNARVVLPLTtdTDKADLLEAIDALKKG-LGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 151 FMQAGFRKAIQQIESFNSGNkVPSMIIAMTDGElVAHAFQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIAD--SPG 227
Cdd:cd00198   81 NIGAALRLALELLKSAKRPN-ARRVIILLTDGE-PNDGPELLAEAARELRKLGITVYTIGIgDDANEDELKEIADktTGG 158


                 ...
gi 767961975 228 HVF 230
Cdd:cd00198  159 AVF 161
VWA pfam00092
von Willebrand factor type A domain;
76-245 3.76e-19

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 84.25  E-value: 3.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975   76 DLYFILDKSGSVNN-NWIDLYMWVEETVARFQ--SPNIRMCFITYSTDGQTVLPLTSDKNR--IKNGLDQLqKIVPDGHT 150
Cdd:pfam00092   1 DIVFLLDGSGSIGGdNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKeeLLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  151 FMQAGFRKAIQQI--ESFNSGNKVPSMIIAMTDGElvaHAFQDTLREAQKARKLGANVYTLGVADYNLDQITAIADSP-- 226
Cdd:pfam00092  80 NTGKALKYALENLfsSAAGARPGAPKVVVLLTDGR---SQDGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPge 156

                         170
                  ....*....|....*....
gi 767961975  227 GHVFAVENgFKALRSTIDA 245
Cdd:pfam00092 157 GHVFTVSD-FEALEDLQDQ 174
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 66-246 4.17e-18

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: 83.45  E-value: 4.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  66 QAGHRCQGSFDLYFILDKSGSvnnnwidlyMWVE-------ETVARF---QSPNIRMCFITYSTDGQTVLPLTSDKNRIK 135
Cdd:COG1240   84 LALARPQRGRDVVLVVDASGS---------MAAEnrleaakGALLDFlddYRPRDRVGLVAFGGEAEVLLPLTRDREALK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 136 NGLDQLQkivPDGHTFMQAGFRKAIQQIESFNSGNKVpsMIIAMTDGElvAHA-FQDTLREAQKARKLGANVYTLGVAD- 213
Cdd:COG1240  155 RALDELP---PGGGTPLGDALALALELLKRADPARRK--VIVLLTDGR--DNAgRIDPLEAAELAAAAGIRIYTIGVGTe 227

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767961975 214 -YNLDQITAIAD-SPGHVFAVENgFKALRSTIDAL 246
Cdd:COG1240  228 aVDEGLLREIAEaTGGRYFRADD-LSELAAIYREI 261
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 76-224 9.85e-16

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 77.06  E-value: 9.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  76 DLYFILDKSGSVNNNWIDLymwVEETVARF--Q-SPNIRMCFITYSTDGQTVLPLTS--DKNRIKNGLDQLQkivPDGHT 150
Cdd:COG2304   93 NLVFVIDVSGSMSGDKLEL---AKEAAKLLvdQlRPGDRVSIVTFAGDARVLLPPTPatDRAKILAAIDRLQ---AGGGT 166

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961975 151 FMQAGFRKAIQQIESFNSGNKVPSMIIaMTDGELVAHA--FQDTLREAQKARKLGANVYTLGV-ADYNLDQITAIAD 224
Cdd:COG2304  167 ALGAGLELAYELARKHFIPGRVNRVIL-LTDGDANVGItdPEELLKLAEEAREEGITLTTLGVgSDYNEDLLERLAD 242
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 76-214 3.98e-12

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: 64.33  E-value: 3.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  76 DLYFILDKSGSVN-NNWIDLYM-WVEETVARFQ-SPN-IRMCFITYSTDGQTVLPLTS----DKNRIKNGLDQLQKI-VP 146
Cdd:cd01471    2 DLYLLVDGSGSIGySNWVTHVVpFLHTFVQNLNiSPDeINLYLVTFSTNAKELIRLSSpnstNKDLALNAIRALLSLyYP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961975 147 DGHTFMQAGFRKAIQQIESFNSG-NKVPSMIIAMTDGElvAHAFQDTLREAQKARKLGANVYTLGVADY 214
Cdd:cd01471   82 NGSTNTTSALLVVEKHLFDTRGNrENAPQLVIIMTDGI--PDSKFRTLKEARKLRERGVIIAVLGVGQG 148
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 76-215 1.23e-11

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 64.70  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  76 DLYFILDKSGSvnnnwidlyM--WVEETVARF-------QSPNIRMCFITYSTDGQTVLPLTSDKnRIKNGLDQLQKIVP 146
Cdd:COG2425  120 PVVLCVDTSGS---------MagSKEAAAKAAalallraLRPNRRFGVILFDTEVVEDLPLTADD-GLEDAIEFLSGLFA 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961975 147 DGHTFMQAGFRKAIQQIESFNSGNKVpsmIIAMTDGElvAHAFQDTLREAQKARKLGANVYTLGVADYN 215
Cdd:COG2425  190 GGGTDIAPALRAALELLEEPDYRNAD---IVLITDGE--AGVSPEELLREVRAKESGVRLFTVAIGDAG 253
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 77-232 2.09e-11

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: 61.91  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  77 LYFILDKSGSVNNNWIDLYMWVEETVARFQSPNIRMCFITYSTDGQTVLPLTS--DKNRIKNGLDQLQkivPDGHTFMQA 154
Cdd:cd01465    3 LVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLPATPvrDKAAILAAIDRLT---AGGSTAGGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 155 GFRKAIQQIESfNSGNKVPSMIIAMTDGEL-VAHAFQDTLRE-AQKARKLGANVYTLGVAD-YNLDQITAIADSPGHVFA 231
Cdd:cd01465   80 GIQLGYQEAQK-HFVPGGVNRILLATDGDFnVGETDPDELARlVAQKRESGITLSTLGFGDnYNEDLMEAIADAGNGNTA 158


                 .
gi 767961975 232 V 232
Cdd:cd01465  159 Y 159
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
78-250 1.41e-10

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 60.32  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  78 YFILDKSGSVNNNWIDLymwVEETVARFQS---------PNIRMCFITYSTDGQTVLPLTSdknrikngLDQLQ--KIVP 146
Cdd:COG4245    9 YLLLDTSGSMSGEPIEA---LNEGLQALIDelrqdpyalETVEVSVITFDGEAKVLLPLTD--------LEDFQppDLSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 147 DGHTFMQAGFRKAIQQIES---FNSGNKVPS---MIIAMTDGELVAHAFQDTLREAQKA-RKLGANVYTLGV-ADYNLDQ 218
Cdd:COG4245   78 SGGTPLGAALELLLDLIERrvqKYTAEGKGDwrpVVFLITDGEPTDSDWEAALQRLKDGeAAKKANIFAIGVgPDADTEV 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767961975 219 ITAIADsPGHVFAVENGfKALRSTIDALTSKV 250
Cdd:COG4245  158 LKQLTD-PVRALDALDG-LDFREFFKWLSASV 187
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 76-234 1.22e-09

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: 56.85  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  76 DLYFILDKSGSVNNNWIDLYM-WVEETVARF-QSPN-IRMCFITYSTDGQTVLPLT--SDKNRIKNGLDQLQKIvpDGHT 150
Cdd:cd01472    2 DIVFLVDGSESIGLSNFNLVKdFVKRVVERLdIGPDgVRVGVVQYSDDPRTEFYLNtyRSKDDVLEAVKNLRYI--GGGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 151 FMQAGFRKAIQQI--ESFNSGNKVPSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADYNLDQITAIADSPG 227
Cdd:cd01472   80 NTGKALKYVRENLftEASGSREGVPKVLVVITDGKS-----QDDVEEpAVELKQAGIEVFAVGVKNADEEELKQIASDPK 154


                 ....*....
gi 767961975 228 --HVFAVEN 234
Cdd:cd01472  155 elYVFNVAD 163
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 76-230 2.15e-08

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: 53.17  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  76 DLYFILDKSGSVNNNWIDLYMWVEETVARFQ-SPN-IRMCFITYSTDGQTVLPLT----SDKNRIKNGLDQLQKIvpDGH 149
Cdd:cd01476    2 DLLFVLDSSGSVRGKFEKYKKYIERIVEGLEiGPTaTRVALITYSGRGRQRVRFNlpkhNDGEELLEKVDNLRFI--GGT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 150 TFMQAGFRKAIQQIESFNSGNK-VPSMIIAMTDGelvaHAFQDTLREAQKARKlGANVYTLGVADY-----NLDQITAIA 223
Cdd:cd01476   80 TATGAAIEVALQQLDPSEGRREgIPKVVVVLTDG----RSHDDPEKQARILRA-VPNIETFAVGTGdpgtvDTEELHSIT 154


                 ....*..
gi 767961975 224 DSPGHVF 230
Cdd:cd01476  155 GNEDHIF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 76-234 7.81e-08

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: 51.52  E-value: 7.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  76 DLYFILDKSGSV-NNNWIDLYMWVEETVARFQ-SPN-IRMCFITYSTDGQTVLPLTSDKNRiKNGLDQLQKI-VPDGHTF 151
Cdd:cd01482    2 DIVFLVDGSWSIgRSNFNLVRSFLSSVVEAFEiGPDgVQVGLVQYSDDPRTEFDLNAYTSK-EDVLAAIKNLpYKGGNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 152 MQAGFRKAIQQIESFNSG--NKVPSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADYNLDQITAIADSPG- 227
Cdd:cd01482   81 TGKALTHVREKNFTPDAGarPGVPKVVILITDGKS-----QDDVELpARVLRNLGVNVFAVGVKDADESELKMIASKPSe 155


                 ....*...
gi 767961975 228 -HVFAVEN 234
Cdd:cd01482  156 tHVFNVAD 163
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 73-274 2.92e-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: 50.85  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  73 GSFDLYFILDKSGSVN-NNWidlymwveETVARFQ---------SPNI-RMCFITYSTDGQTVLPLTSDKNRiKNGLDQL 141
Cdd:cd01475    1 GPTDLVFLIDSSRSVRpENF--------ELVKQFLnqiidsldvGPDAtRVGLVQYSSTVKQEFPLGRFKSK-ADLKRAV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 142 QKIVPDGHTFM-----QAGFRKAIQQIESFNSGN-KVPSMIIAMTDGELvahafQDTLRE-AQKARKLGANVYTLGVADY 214
Cdd:cd01475   72 RRMEYLETGTMtglaiQYAMNNAFSEAEGARPGSeRVPRVGIVVTDGRP-----QDDVSEvAAKARALGIEMFAVGVGRA 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961975 215 NLDQITAIADSP--GHVFAVENgFkalrSTIDALTSK----VCLDvtsvepSSECVGEPyHVVIHG 274
Cdd:cd01475  147 DEEELREIASEPlaDHVFYVED-F----STIEELTKKfqgkICVV------PDLCATLS-HVCQQV 200
VWA_2 pfam13519
von Willebrand factor type A domain;
77-177 1.74e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 46.13  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975   77 LYFILDKSGSVNNNWIDLYMW--VEETVARF--QSPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQkiVPDGHTFM 152
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLeaAKDAVLALlkSLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLE--PKGGGTNL 78

                          90       100
                  ....*....|....*....|....*
gi 767961975  153 QAGFRKAIQQIesFNSGNKVPSMII 177
Cdd:pfam13519  79 AAALQLARAAL--KHRRKNQPRRIV 101
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 76-212 8.87e-06

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


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 45.46  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  76 DLYFILDKSGSVNNNWIDLYMWVEETVARFQSPNIRMCFITYSTDGQTVLPL----TSDKNRIKNGLDQLQkivPDGHTF 151
Cdd:cd01466    2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSPLrrmtAKGKRSAKRVVDGLQ---AGGGTN 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767961975 152 MQAGFRKAIQQIESFNSGNKVPSmIIAMTDGElVAHAFQDTlreaqKARKLGANVYTLGVA 212
Cdd:cd01466   79 VVGGLKKALKVLGDRRQKNPVAS-IMLLSDGQ-DNHGAVVL-----RADNAPIPIHTFGLG 132
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 76-236 8.05e-05

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: 43.09  E-value: 8.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  76 DLYFILDKSGSVNN------NWIDLymwVEETVARF--QSPNIRMCFITYSTDGQTVLPLTSDKNRIKNGLDQLQKIVPD 147
Cdd:cd01467    4 DIMIALDVSGSMLAqdfvkpSRLEA---AKEVLSDFidRRENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGLAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 148 GHTFMQAGFRKAIQQIESFNSGNKVpsmIIAMTDGELVAhAFQDTLREAQKARKLGANVYTLGVADY------------N 215
Cdd:cd01467   81 QGTAIGDAIGLAIKRLKNSEAKERV---IVLLTDGENNA-GEIDPATAAELAKNKGVRIYTIGVGKSgsgpkpdgstilD 156

                        170       180
                 ....*....|....*....|..
gi 767961975 216 LDQITAIAD-SPGHVFAVENGF 236
Cdd:cd01467  157 EDSLVEIADkTGGRIFRALDGF 178
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 76-210 8.43e-04

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 39.89  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  76 DLYFILDKSGSVNNNWIdlyMWVEETVARFQS---PNIRMCFITYSTDGQTVLP--LTSDKNRIKNGLDQLQKIVPDGHT 150
Cdd:cd01461    4 EVVFVIDTSGSMSGTKI---EQTKEALLTALKdlpPGDYFNIIGFSDTVEEFSPssVSATAENVAAAIEYVNRLQALGGT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975 151 FMQAGFRKAIQQIesfNSGNKVPSMIIAMTDGElVAHAFQdTLREAQKARKLGANVYTLG 210
Cdd:cd01461   81 NMNDALEAALELL---NSSPGSVPQIILLTDGE-VTNESQ-ILKNVREALSGRIRLFTFG 135
vWA_ORF176_type cd01457
VWA ORF176 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 75-183 1.95e-03

VWA ORF176 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. The members of this subgroup are Eubacterial in origin and have a conserved MIDAS motif. Not much is known about the biochemistry of these.


Pssm-ID: 238734  Cd Length: 199  Bit Score: 39.01  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961975  75 FDLYFILDKSGSVnnnwidlyMWVEET--VARFQSPN------IRMCFItYSTDGQTVLPLTSDKNRIKN----GLDQL- 141
Cdd:cd01457    3 RDYTLLIDKSGSM--------AEADEAkeRSRWEEAQestralARKCEE-YDSDGITVYLFSGDFRRYDNvnssKVDQLf 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767961975 142 QKIVPDGHTFMQAGFRKAIQQ-IESFNSGNKVPSM--IIAMTDGE 183
Cdd:cd01457   74 AENSPDGGTNLAAVLQDALNNyFQRKENGATCPEGetFLVITDGA 118
 
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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