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Conserved domains on  [gi|1039746122|ref|XP_017171500|]
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anthrax toxin receptor-like isoform X3 [Mus musculus]

Protein Classification

vWA_ATR and Anth_Ig domain-containing protein( domain architecture ID 10107122)

vWA_ATR and Anth_Ig domain-containing protein

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, ...
 14-198 3.45e-108

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: 324.08  E-value: 3.45e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  14 CQGIFDLYLVLDKSGSVADNWIHIYSFAEGLVKKFTNPNLRISIITYSTEAEVILPLTSDSKEINKSLLVLKNIVPQGLT 93
Cdd:cd01474     1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  94 HMQKGLRKANEQIRKSTLGGRIVNSVIIALTDGLLLLKPYLDTMEEAKKARRMGAIVYTVGVFMYSKQQLVNIAGDPDRC 173
Cdd:cd01474    81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                         170       180
                  ....*....|....*....|....*
gi 1039746122 174 FGVDEGFSALEGVVDPLTSKSCTEI 198
Cdd:cd01474   161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 193-294 1.67e-43

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: 151.25  E-value: 1.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122 193 KSCTEILSVQPTYVCAKDFYQVNISGHGLNNTSNMKQVICRFKFSDSKVVDESPSDMNEHSITCPGPKIKHTGEDVSLQV 272
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|..
gi 1039746122 273 SLNNGISFIGNKLIITSTNCWS 294
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCSD 102
PRK08581 super family cl35718
amidase domain-containing protein;
301-356 6.19e-03

amidase domain-containing protein;


The actual alignment was detected with superfamily member PRK08581:

Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 39.77  E-value: 6.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746122 301 TATDTTSQSTATDTTSQSTATDTTSQSTATDTTSQSTARDTTSQPQKKDPDKVSAT 356
Cdd:PRK08581   26 YADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTI 81
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 14-198 3.45e-108

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: 324.08  E-value: 3.45e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  14 CQGIFDLYLVLDKSGSVADNWIHIYSFAEGLVKKFTNPNLRISIITYSTEAEVILPLTSDSKEINKSLLVLKNIVPQGLT 93
Cdd:cd01474     1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  94 HMQKGLRKANEQIRKSTLGGRIVNSVIIALTDGLLLLKPYLDTMEEAKKARRMGAIVYTVGVFMYSKQQLVNIAGDPDRC 173
Cdd:cd01474    81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                         170       180
                  ....*....|....*....|....*
gi 1039746122 174 FGVDEGFSALEGVVDPLTSKSCTEI 198
Cdd:cd01474   161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 193-294 1.67e-43

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: 151.25  E-value: 1.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122 193 KSCTEILSVQPTYVCAKDFYQVNISGHGLNNTSNMKQVICRFKFSDSKVVDESPSDMNEHSITCPGPKIKHTGEDVSLQV 272
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|..
gi 1039746122 273 SLNNGISFIGNKLIITSTNCWS 294
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCSD 102
VWA pfam00092
von Willebrand factor type A domain;
19-188 8.93e-23

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 95.80  E-value: 8.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSV-ADNWIHIYSFAEGLVKKFT--NPNLRISIITYSTEAEVILPLT--SDSKEINKSllvLKNIVPQ--G 91
Cdd:pfam00092   1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNdySSKEELLSA---VDNLRYLggG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  92 LTHMQKGLRKANEQIRKSTLGGRI-VNSVIIALTDGllllKPY-LDTMEEAKKARRMGAIVYTVGV-FMYSKqQLVNIAG 168
Cdd:pfam00092  78 TTNTGKALKYALENLFSSAAGARPgAPKVVVLLTDG----RSQdGDPEEVARELKSAGVTVFAVGVgNADDE-ELRKIAS 152

                         170       180
                  ....*....|....*....|..
gi 1039746122 169 DPDRC--FGVDEgFSALEGVVD 188
Cdd:pfam00092 153 EPGEGhvFTVSD-FEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 19-172 7.84e-21

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: 90.21  E-value: 7.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122   19 DLYLVLDKSGSVADNWIHIY-SFAEGLVKKFT--NPNLRISIITYSTEAEVILPL--TSDSKEINKsllVLKNIVPQ--G 91
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAkEFVLKLVEQLDigPDGDRVGLVTFSDDARVLFPLndSRSKDALLE---ALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122   92 LTHMQKGLRKANEQIRKSTLGGRI-VNSVIIALTDGllllKP---YLDTMEEAKKARRMGAIVYTVGV-FMYSKQQLVNI 166
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRgAPKVVILITDG----ESndgPKDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKL 153


                   ....*.
gi 1039746122  167 AGDPDR 172
Cdd:smart00327 154 ASAPGG 159
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 19-155 3.53e-17

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: 81.91  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGS-VADNWIhiySFAEGLVKKFTN---PNLRISIITYSTEAEVILPLTSDSKEINKSllvLKNIVPQGLTH 94
Cdd:COG1240    94 DVVLVVDASGSmAAENRL---EAAKGALLDFLDdyrPRDRVGLVAFGGEAEVLLPLTRDREALKRA---LDELPPGGGTP 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746122  95 MQKGLRKANEQIRKSTLGGRivnSVIIALTDGllllKP---YLDTMEEAKKARRMGAIVYTVGV 155
Cdd:COG1240   168 LGDALALALELLKRADPARR---KVIVLLTDG----RDnagRIDPLEAAELAAAAGIRIYTIGV 224
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 14-198 2.24e-07

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 53.81  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  14 CQGIFDLYLVLDKSGSVA-DNWI-HIYSFAEGLVKKFT----NPNLRISIitYSTEAEVILPLTSD-SKEINKSLLVLKN 86
Cdd:PTZ00441   39 CNEEVDLYLLVDGSGSIGyHNWItHVIPMLMGLIQQLNlsddAINLYMSL--FSNNTTELIRLGSGaSKDKEQALIIVKS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  87 I----VPQGLTHMQKGLrkanEQIRKStLGGRI----VNSVIIALTDGLLLLKpyLDTMEEAKKARRMGAIVYTVGVfmy 158
Cdd:PTZ00441  117 LrktyLPYGKTNMTDAL----LEVRKH-LNDRVnrenAIQLVILMTDGIPNSK--YRALEESRKLKDRNVKLAVIGI--- 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039746122 159 skQQLVN------IAG----DPDRCFGVDEGFSALEGVVDPLTSKSCTEI 198
Cdd:PTZ00441  187 --GQGINhqfnrlLAGcrprEGKCKFYSDADWEEAKNLIKPFIAKVCTEV 234
PRK08581 PRK08581
amidase domain-containing protein;
301-356 6.19e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 39.77  E-value: 6.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746122 301 TATDTTSQSTATDTTSQSTATDTTSQSTATDTTSQSTARDTTSQPQKKDPDKVSAT 356
Cdd:PRK08581   26 YADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTI 81
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 14-198 3.45e-108

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: 324.08  E-value: 3.45e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  14 CQGIFDLYLVLDKSGSVADNWIHIYSFAEGLVKKFTNPNLRISIITYSTEAEVILPLTSDSKEINKSLLVLKNIVPQGLT 93
Cdd:cd01474     1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  94 HMQKGLRKANEQIRKSTLGGRIVNSVIIALTDGLLLLKPYLDTMEEAKKARRMGAIVYTVGVFMYSKQQLVNIAGDPDRC 173
Cdd:cd01474    81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                         170       180
                  ....*....|....*....|....*
gi 1039746122 174 FGVDEGFSALEGVVDPLTSKSCTEI 198
Cdd:cd01474   161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 193-294 1.67e-43

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: 151.25  E-value: 1.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122 193 KSCTEILSVQPTYVCAKDFYQVNISGHGLNNTSNMKQVICRFKFSDSKVVDESPSDMNEHSITCPGPKIKHTGEDVSLQV 272
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|..
gi 1039746122 273 SLNNGISFIGNKLIITSTNCWS 294
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCSD 102
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 18-172 1.69e-28

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: 111.61  E-value: 1.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  18 FDLYLVLDKSGSVA-DNWIHIYSFAEGLVKKFTNP--NLRISIITYSTEAEVILPLTSDS--KEINKSLLVLKNIVPQGl 92
Cdd:cd01450     1 LDIVFLLDGSESVGpENFEKVKDFIEKLVEKLDIGpdKTRVGLVQYSDDVRVEFSLNDYKskDDLLKAVKNLKYLGGGG- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  93 THMQKGLRKANEQIRKSTLGGRIVNSVIIALTDGllllKPYLDTM--EEAKKARRMGAIVYTVGVFMYSKQQLVNIAGDP 170
Cdd:cd01450    80 TNTGKALQYALEQLFSESNARENVPKVIIVLTDG----RSDDGGDpkEAAAKLKDEGIKVFVVGVGPADEEELREIASCP 155


                  ..
gi 1039746122 171 DR 172
Cdd:cd01450   156 SE 157
VWA pfam00092
von Willebrand factor type A domain;
19-188 8.93e-23

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 95.80  E-value: 8.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSV-ADNWIHIYSFAEGLVKKFT--NPNLRISIITYSTEAEVILPLT--SDSKEINKSllvLKNIVPQ--G 91
Cdd:pfam00092   1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNdySSKEELLSA---VDNLRYLggG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  92 LTHMQKGLRKANEQIRKSTLGGRI-VNSVIIALTDGllllKPY-LDTMEEAKKARRMGAIVYTVGV-FMYSKqQLVNIAG 168
Cdd:pfam00092  78 TTNTGKALKYALENLFSSAAGARPgAPKVVVLLTDG----RSQdGDPEEVARELKSAGVTVFAVGVgNADDE-ELRKIAS 152

                         170       180
                  ....*....|....*....|..
gi 1039746122 169 DPDRC--FGVDEgFSALEGVVD 188
Cdd:pfam00092 153 EPGEGhvFTVSD-FEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 19-172 7.84e-21

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: 90.21  E-value: 7.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122   19 DLYLVLDKSGSVADNWIHIY-SFAEGLVKKFT--NPNLRISIITYSTEAEVILPL--TSDSKEINKsllVLKNIVPQ--G 91
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAkEFVLKLVEQLDigPDGDRVGLVTFSDDARVLFPLndSRSKDALLE---ALASLSYKlgG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122   92 LTHMQKGLRKANEQIRKSTLGGRI-VNSVIIALTDGllllKP---YLDTMEEAKKARRMGAIVYTVGV-FMYSKQQLVNI 166
Cdd:smart00327  78 GTNLGAALQYALENLFSKSAGSRRgAPKVVILITDG----ESndgPKDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKL 153


                   ....*.
gi 1039746122  167 AGDPDR 172
Cdd:smart00327 154 ASAPGG 159
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 19-172 7.73e-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: 86.85  E-value: 7.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSVADNWIHI-YSFAEGLVKKFTN--PNLRISIITYSTEAEVILPLTSD-SKEINKSLLVLKNIVPQGLTH 94
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKaKEALKALVSSLSAspPGDRVGLVTFGSNARVVLPLTTDtDKADLLEAIDALKKGLGGGTN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746122  95 MQKGLRKANEQIRKSTLGGRivNSVIIALTDGlLLLKPYLDTMEEAKKARRMGAIVYTVGVFM-YSKQQLVNIAGDPDR 172
Cdd:cd00198    82 IGAALRLALELLKSAKRPNA--RRVIILLTDG-EPNDGPELLAEAARELRKLGITVYTIGIGDdANEDELKEIADKTTG 157
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 19-158 7.46e-18

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: 82.05  E-value: 7.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSVA-DNWI-HIYSFAEGLVKKF--TNPNLRISIITYSTEAEVILPLtSDSKEINKSLL------VLKNIV 88
Cdd:cd01471     2 DLYLLVDGSGSIGySNWVtHVVPFLHTFVQNLniSPDEINLYLVTFSTNAKELIRL-SSPNSTNKDLAlnairaLLSLYY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746122  89 PQGLTHMQKGLRKAnEQIRKSTLGGR-IVNSVIIALTDGLLLLKPylDTMEEAKKARRMGAIVYTVGVFMY 158
Cdd:cd01471    81 PNGSTNTTSALLVV-EKHLFDTRGNReNAPQLVIIMTDGIPDSKF--RTLKEARKLRERGVIIAVLGVGQG 148
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 19-155 3.53e-17

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: 81.91  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGS-VADNWIhiySFAEGLVKKFTN---PNLRISIITYSTEAEVILPLTSDSKEINKSllvLKNIVPQGLTH 94
Cdd:COG1240    94 DVVLVVDASGSmAAENRL---EAAKGALLDFLDdyrPRDRVGLVAFGGEAEVLLPLTRDREALKRA---LDELPPGGGTP 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039746122  95 MQKGLRKANEQIRKSTLGGRivnSVIIALTDGllllKP---YLDTMEEAKKARRMGAIVYTVGV 155
Cdd:COG1240   168 LGDALALALELLKRADPARR---KVIVLLTDG----RDnagRIDPLEAAELAAAAGIRIYTIGV 224
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 19-155 5.49e-12

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 67.05  E-value: 5.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSVADN-WIHIYSFAEGLVKKFtNPNLRISIITYSTEAEVILPLTS--DSKEINKSllvLKNIVPQGLTHM 95
Cdd:COG2304    93 NLVFVIDVSGSMSGDkLELAKEAAKLLVDQL-RPGDRVSIVTFAGDARVLLPPTPatDRAKILAA---IDRLQAGGGTAL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746122  96 QKGLRKANEQIRKSTLGGRIvNSVIIaLTDGLLLLKP-YLDTMEE-AKKARRMGAIVYTVGV 155
Cdd:COG2304   169 GAGLELAYELARKHFIPGRV-NRVIL-LTDGDANVGItDPEELLKlAEEAREEGITLTTLGV 228
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 19-169 1.18e-10

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 62.39  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSVADNWIHI-YSFAEGLVKKFtNPNLRISIITYSTEAEVILPLTSDsKEINKSLLVLKNIVPQGLTHMQK 97
Cdd:COG2425   120 PVVLCVDTSGSMAGSKEAAaKAAALALLRAL-RPNRRFGVILFDTEVVEDLPLTAD-DGLEDAIEFLSGLFAGGGTDIAP 197

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039746122  98 GLRKANEQIRKSTLGGRIVnsVIIalTDGLLLLKPYlDTMEEAkKARRMGAIVYTVGVFMYSKQQLVNIAGD 169
Cdd:COG2425   198 ALRAALELLEEPDYRNADI--VLI--TDGEAGVSPE-ELLREV-RAKESGVRLFTVAIGDAGNPGLLEALAD 263
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
21-155 2.57e-09

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 57.24  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  21 YLVLDKSGSVADNWIH-----IYSFAEGLVK-KFTNPNLRISIITYSTEAEVILPLTSdskeinKSLLVLKNIVPQGLTH 94
Cdd:COG4245     9 YLLLDTSGSMSGEPIEalnegLQALIDELRQdPYALETVEVSVITFDGEAKVLLPLTD------LEDFQPPDLSASGGTP 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039746122  95 MQKGLRKANEQIRK-----STLGGRIVNSVIIALTDGllllKPYLDTMEEAKKA-----RRMGAIVYTVGV 155
Cdd:COG4245    83 LGAALELLLDLIERrvqkyTAEGKGDWRPVVFLITDG----EPTDSDWEAALQRlkdgeAAKKANIFAIGV 149
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 19-170 3.10e-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: 56.47  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSVA-DNWIHIYSFAEGLVKKFTNPNL--RISIITYSTEAEVILPLTSDSKeiNKSLLV-LKNIVPQG-LT 93
Cdd:cd01472     2 DIVFLVDGSESIGlSNFNLVKDFVKRVVERLDIGPDgvRVGVVQYSDDPRTEFYLNTYRS--KDDVLEaVKNLRYIGgGT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039746122  94 HMQKGLRKANEQIRKSTLGGRI-VNSVIIALTDGllllKPYLDTMEEAKKARRMGAIVYTVGVFMYSKQQLVNIAGDP 170
Cdd:cd01472    80 NTGKALKYVRENLFTEASGSREgVPKVLVVITDG----KSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIASDP 153
VWA_2 pfam13519
von Willebrand factor type A domain;
20-123 4.64e-09

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 54.22  E-value: 4.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  20 LYLVLDKSGSVAD------NWIHIYSFAEGLVKKftNPNLRISIITYSTEAEVILPLTSDSKEINKSllvLKNIVP-QGL 92
Cdd:pfam13519   1 LVFVLDTSGSMRNgdygptRLEAAKDAVLALLKS--LPGDRVGLVTFGDGPEVLIPLTKDRAKILRA---LRRLEPkGGG 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039746122  93 THMQKGLRKANEQIRKSTLGGRivnSVIIAL 123
Cdd:pfam13519  76 TNLAAALQLARAALKHRRKNQP---RRIVLI 103
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 20-126 2.07e-08

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: 54.20  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  20 LYLVLDKSGSVADNWIH-IYSFAEGLVKKFtNPNLRISIITYSTEAEVILPLTS--DSKEINKSllvLKNIVPQGLTHMQ 96
Cdd:cd01465     3 LVFVIDRSGSMDGPKLPlVKSALKLLVDQL-RPDDRLAIVTYDGAAETVLPATPvrDKAAILAA---IDRLTAGGSTAGG 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039746122  97 KGLRKANEQIRKSTLGGRIvnSVIIALTDG 126
Cdd:cd01465    79 AGIQLGYQEAQKHFVPGGV--NRILLATDG 106
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 14-198 2.24e-07

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 53.81  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  14 CQGIFDLYLVLDKSGSVA-DNWI-HIYSFAEGLVKKFT----NPNLRISIitYSTEAEVILPLTSD-SKEINKSLLVLKN 86
Cdd:PTZ00441   39 CNEEVDLYLLVDGSGSIGyHNWItHVIPMLMGLIQQLNlsddAINLYMSL--FSNNTTELIRLGSGaSKDKEQALIIVKS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  87 I----VPQGLTHMQKGLrkanEQIRKStLGGRI----VNSVIIALTDGLLLLKpyLDTMEEAKKARRMGAIVYTVGVfmy 158
Cdd:PTZ00441  117 LrktyLPYGKTNMTDAL----LEVRKH-LNDRVnrenAIQLVILMTDGIPNSK--YRALEESRKLKDRNVKLAVIGI--- 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039746122 159 skQQLVN------IAG----DPDRCFGVDEGFSALEGVVDPLTSKSCTEI 198
Cdd:PTZ00441  187 --GQGINhqfnrlLAGcrprEGKCKFYSDADWEEAKNLIKPFIAKVCTEV 234
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 19-174 2.38e-07

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: 50.86  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSVADNWIHIYSFAEGLVKKFTNPN--LRISIITYSTEA----EVILPLTSDSKEINKSLLVLKNIvpQGL 92
Cdd:cd01476     2 DLLFVLDSSGSVRGKFEKYKKYIERIVEGLEIGPtaTRVALITYSGRGrqrvRFNLPKHNDGEELLEKVDNLRFI--GGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  93 THMQKGLRKANEQIRKSTLGGRIVNSVIIALTDGllllKPYLDTMEEAKKARRM-GAIVYTVGVFMYS---KQQLVNIAG 168
Cdd:cd01476    80 TATGAAIEVALQQLDPSEGRREGIPKVVVVLTDG----RSHDDPEKQARILRAVpNIETFAVGTGDPGtvdTEELHSITG 155


                  ....*.
gi 1039746122 169 DPDRCF 174
Cdd:cd01476   156 NEDHIF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 19-170 7.42e-07

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: 50.08  E-value: 7.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSVADNWIHIY-SFAEGLVKKF------TNPNL--RISIITYSTEAEVILPLT---SDSKEINKSLLVLKN 86
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITkNFVKRVAERFlkdyyrKDPAGswRVGVVQYSDQQEVEAGFLrdiRNYTSLKEAVDNLEY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  87 IvpQGLTHMQKGLRKANEQIRKSTLGGriVNSVIIALTDGllllKPY-------LDTMEEAKKArrmGAIVYTVGVFMYS 159
Cdd:cd01480    84 I--GGGTFTDCALKYATEQLLEGSHQK--ENKFLLVITDG----HSDgspdggiEKAVNEADHL---GIKIFFVAVGSQN 152

                         170
                  ....*....|.
gi 1039746122 160 KQQLVNIAGDP 170
Cdd:cd01480   153 EEPLSRIACDG 163
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 19-126 3.67e-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: 47.38  E-value: 3.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSVADNWIHIYSFAEGLVKKFTNPNLRISIITYSTEAEVILPL---TSDSKEINKSLLVlkNIVPQGLTHM 95
Cdd:cd01466     2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSPLrrmTAKGKRSAKRVVD--GLQAGGGTNV 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039746122  96 QKGLRKANEQIRKSTLGGRIVNsvIIALTDG 126
Cdd:cd01466    80 VGGLKKALKVLGDRRQKNPVAS--IMLLSDG 108
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 15-155 8.33e-06

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: 46.55  E-value: 8.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  15 QGIfDLYLVLDKSGSV-ADNWIHI--YSFAEGLVKKFTN--PNLRISIITYSTEAEVILPLTSDSKEINKSLLVLKNIVP 89
Cdd:cd01467     1 EGR-DIMIALDVSGSMlAQDFVKPsrLEAAKEVLSDFIDrrENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGLA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039746122  90 QGLTHMQKGLRKANEQIRKSTLGGRivnsVIIALTDGLL---LLKPylDTMEEAKKARrmGAIVYTVGV 155
Cdd:cd01467    80 GQGTAIGDAIGLAIKRLKNSEAKER----VIVLLTDGENnagEIDP--ATAAELAKNK--GVRIYTIGV 140
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 21-126 8.90e-06

VWA subfamily: 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 have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 46.56  E-value: 8.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  21 YLVLDKSGSVADNWIHiySFAEGL------VKKftNP----NLRISIITYSTEAEVILPLTSDSKEINKSLLVlknivpQ 90
Cdd:cd01464     7 YLLLDTSGSMAGEPIE--ALNQGLqmlqseLRQ--DPyaleSVEISVITFDSAARVIVPLTPLESFQPPRLTA------S 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039746122  91 GLTHMQKGLRKA----NEQIRKSTlGGRIVN--SVIIALTDG 126
Cdd:cd01464    77 GGTSMGAALELAldciDRRVQRYR-ADQKGDwrPWVFLLTDG 117
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 18-168 1.45e-04

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 43.07  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  18 FDLYLVLDKSGSV-ADNWI-HIYSFAEGLVKKFT--NPNLRISIITYSTEAEVILPLTSDSKEINKSLLVL-----KNIV 88
Cdd:cd01473     1 YDLTLILDESASIgYSNWRkDVIPFTEKIINNLNisKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKindlkNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  89 PQGLTHMQKGLRKANEQIRKStlGGRIVNS--VIIALTDGllllkpyLDTMEEAKKARRMGaIVYT--------VGVFMY 158
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKH--GNRRKDApkVTMLFTDG-------NDTSASKKELQDIS-LLYKeenvkllvVGVGAA 150

                         170
                  ....*....|
gi 1039746122 159 SKQQLVNIAG 168
Cdd:cd01473   151 SENKLKLLAG 160
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 19-127 1.57e-03

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 40.35  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSVADNWIHIY-SFAEGLVKKFTN--PNLRISIITYSTEAEVILPLT-SDSKEINKSLLVLKNI------V 88
Cdd:cd01470     2 NIYIALDASDSIGEEDFDEAkNAIKTLIEKISSyeVSPRYEIISYASDPKEIVSIRdFNSNDADDVIKRLEDFnyddhgD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039746122  89 PQGlTHMQKGLRK-----ANEQIRKSTLGGRIVNsVIIALTDGL 127
Cdd:cd01470    82 KTG-TNTAAALKKvyermALEKVRNKEAFNETRH-VIILFTDGK 123
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 19-197 3.87e-03

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: 39.29  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  19 DLYLVLDKSGSVADnwihiYSFAegLVKKFTN---------PNL-RISIITYSTEAEVILPLTSDS--KEINKSLLVLKn 86
Cdd:cd01475     4 DLVFLIDSSRSVRP-----ENFE--LVKQFLNqiidsldvgPDAtRVGLVQYSSTVKQEFPLGRFKskADLKRAVRRME- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039746122  87 ivpqgltHMQKG------LRKANEQIRKSTLGGR----IVNSVIIALTDGllllKPYLDTMEEAKKARRMGAIVYTVGVF 156
Cdd:cd01475    76 -------YLETGtmtglaIQYAMNNAFSEAEGARpgseRVPRVGIVVTDG----RPQDDVSEVAAKARALGIEMFAVGVG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1039746122 157 MYSKQQLVNIAGDP--DRCFGVdEGFSALEGVVDPLTSKSCTE 197
Cdd:cd01475   145 RADEEELREIASEPlaDHVFYV-EDFSTIEELTKKFQGKICVV 186
PRK08581 PRK08581
amidase domain-containing protein;
301-356 6.19e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 39.77  E-value: 6.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039746122 301 TATDTTSQSTATDTTSQSTATDTTSQSTATDTTSQSTARDTTSQPQKKDPDKVSAT 356
Cdd:PRK08581   26 YADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTI 81
 
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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