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Conserved domains on  [gi|16933553|ref|NP_060623|]
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anthrax toxin receptor 1 isoform 3 precursor [Homo sapiens]

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, ...
 39-223 2.10e-119

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: 341.80  E-value: 2.10e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  39 CYGGFDLYFILDKSGSVLHHWNEIYYFVEQLAHKFISPQLRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQKVLPGGDT 118
Cdd:cd01474   1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 119 YMHEGFERASEQIYYENRQGYRTASVIIALTDGELHEDLFFYSEREANRSRDLGAIVYCVGVKDFNETQLARIADSKDHV 198
Cdd:cd01474  81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                       170       180
                ....*....|....*....|....*
gi 16933553 199 FPVNDGFQALQGIIHSILKKSCIEI 223
Cdd:cd01474 161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 218-318 1.84e-57

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: 180.91  E-value: 1.84e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553   218 KSCIEILAAEPSTICAGESFQVVVRGNGFRHARNVDRVLCSFKINDSVTLNEKPFSVEDTYLLCPAPILKEVGMKAALQV 297
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|.
gi 16933553   298 SMNDGLSFISSSVIITTTHCS 318
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, ...
 39-223 2.10e-119

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: 341.80  E-value: 2.10e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  39 CYGGFDLYFILDKSGSVLHHWNEIYYFVEQLAHKFISPQLRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQKVLPGGDT 118
Cdd:cd01474   1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 119 YMHEGFERASEQIYYENRQGYRTASVIIALTDGELHEDLFFYSEREANRSRDLGAIVYCVGVKDFNETQLARIADSKDHV 198
Cdd:cd01474  81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                       170       180
                ....*....|....*....|....*
gi 16933553 199 FPVNDGFQALQGIIHSILKKSCIEI 223
Cdd:cd01474 161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 218-318 1.84e-57

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: 180.91  E-value: 1.84e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553   218 KSCIEILAAEPSTICAGESFQVVVRGNGFRHARNVDRVLCSFKINDSVTLNEKPFSVEDTYLLCPAPILKEVGMKAALQV 297
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|.
gi 16933553   298 SMNDGLSFISSSVIITTTHCS 318
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCS 101
VWA pfam00092
von Willebrand factor type A domain;
44-212 1.91e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 92.34  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553    44 DLYFILDKSGSV-LHHWNEIYYFVEQLAHKF-ISPQL-RMSFIVFSTRGTTLMKLTE--DREQIRQGLEELqKVLPGGDT 118
Cdd:pfam00092   1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLdIGPDGtRVGLVQYSSDVRTEFPLNDysSKEELLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553   119 YMHEGFERASEQIYYEnRQGYRT--ASVIIALTDGELHEDlffYSEREANRSRDLGAIVYCVGVKDFNETQLARIADSKD 196
Cdd:pfam00092  80 NTGKALKYALENLFSS-AAGARPgaPKVVVLLTDGRSQDG---DPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPG 155

                         170
                  ....*....|....*...
gi 16933553   197 --HVFPVNDgFQALQGII 212
Cdd:pfam00092 156 egHVFTVSD-FEALEDLQ 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 44-212 3.86e-19

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: 83.27  E-value: 3.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553     44 DLYFILDKSGSVLH-HWNEIYYFVEQLAHKF-ISPQL-RMSFIVFSTRGTTLMKL--TEDREQIRQGLEELQKVLpGGDT 118
Cdd:smart00327   1 DVVFLLDGSGSMGGnRFELAKEFVLKLVEQLdIGPDGdRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYKL-GGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553    119 YMHEGFERASEQIYYENRQGYRTA-SVIIALTDGElHEDLFFYSEREANRSRDLGAIVYCVGVK-DFNETQLARIADSKD 196
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGApKVVILITDGE-SNDGPKDLLKAAKELKRSGVKVFVVGVGnDVDEEELKKLASAPG 158

                          170
                   ....*....|....*..
gi 16933553    197 HVF-PVNDGFQALQGII 212
Cdd:smart00327 159 GVYvFLPELLDLLIDLL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 42-215 2.88e-14

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 71.51  E-value: 2.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  42 GFDLYFILDKSGS--VLHHWNEIYYFVEQLAHKFiSPQLRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQkvlPGGDTY 119
Cdd:COG1240  92 GRDVVLVVDASGSmaAENRLEAAKGALLDFLDDY-RPRDRVGLVAFGGEAEVLLPLTRDREALKRALDELP---PGGGTP 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 120 MHEGFERASEQIYYENRQGYRtasVIIALTDGELH---EDLffysEREANRSRDLGAIVYCVGVKD--FNETQLARIADS 194
Cdd:COG1240 168 LGDALALALELLKRADPARRK---VIVLLTDGRDNagrIDP----LEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEA 240

                       170       180
                ....*....|....*....|..
gi 16933553 195 KD-HVFPVNDgFQALQGIIHSI 215
Cdd:COG1240 241 TGgRYFRADD-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, ...
 39-223 2.10e-119

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: 341.80  E-value: 2.10e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  39 CYGGFDLYFILDKSGSVLHHWNEIYYFVEQLAHKFISPQLRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQKVLPGGDT 118
Cdd:cd01474   1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 119 YMHEGFERASEQIYYENRQGYRTASVIIALTDGELHEDLFFYSEREANRSRDLGAIVYCVGVKDFNETQLARIADSKDHV 198
Cdd:cd01474  81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                       170       180
                ....*....|....*....|....*
gi 16933553 199 FPVNDGFQALQGIIHSILKKSCIEI 223
Cdd:cd01474 161 FPVTSGFQALSGIIESVVKKACIEI 185
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 218-318 1.84e-57

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: 180.91  E-value: 1.84e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553   218 KSCIEILAAEPSTICAGESFQVVVRGNGFRHARNVDRVLCSFKINDSVTLNEKPFSVEDTYLLCPAPILKEVGMKAALQV 297
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTINETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDVLV 80

                          90       100
                  ....*....|....*....|.
gi 16933553   298 SMNDGLSFISSSVIITTTHCS 318
Cdd:pfam05587  81 SLNNGKSFISSSLTITATTCS 101
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 43-199 7.50e-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: 106.22  E-value: 7.50e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  43 FDLYFILDKSGSV-LHHWNEIYYFVEQLAHKF-ISP-QLRMSFIVFSTRGTTLMKLTE--DREQIRQGLEELQKVLpGGD 117
Cdd:cd01450   1 LDIVFLLDGSESVgPENFEKVKDFIEKLVEKLdIGPdKTRVGLVQYSDDVRVEFSLNDykSKDDLLKAVKNLKYLG-GGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 118 TYMHEGFERASEQIYYENRQGYRTASVIIALTDGELHEDLffYSEREANRSRDLGAIVYCVGVKDFNETQLARIAD--SK 195
Cdd:cd01450  80 TNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGG--DPKEAAAKLKDEGIKVFVVGVGPADEEELREIAScpSE 157


                ....
gi 16933553 196 DHVF 199
Cdd:cd01450 158 RHVF 161
VWA pfam00092
von Willebrand factor type A domain;
44-212 1.91e-22

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 92.34  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553    44 DLYFILDKSGSV-LHHWNEIYYFVEQLAHKF-ISPQL-RMSFIVFSTRGTTLMKLTE--DREQIRQGLEELqKVLPGGDT 118
Cdd:pfam00092   1 DIVFLLDGSGSIgGDNFEKVKEFLKKLVESLdIGPDGtRVGLVQYSSDVRTEFPLNDysSKEELLSAVDNL-RYLGGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553   119 YMHEGFERASEQIYYEnRQGYRT--ASVIIALTDGELHEDlffYSEREANRSRDLGAIVYCVGVKDFNETQLARIADSKD 196
Cdd:pfam00092  80 NTGKALKYALENLFSS-AAGARPgaPKVVVLLTDGRSQDG---DPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPG 155

                         170
                  ....*....|....*...
gi 16933553   197 --HVFPVNDgFQALQGII 212
Cdd:pfam00092 156 egHVFTVSD-FEALEDLQ 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 44-212 3.86e-19

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: 83.27  E-value: 3.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553     44 DLYFILDKSGSVLH-HWNEIYYFVEQLAHKF-ISPQL-RMSFIVFSTRGTTLMKL--TEDREQIRQGLEELQKVLpGGDT 118
Cdd:smart00327   1 DVVFLLDGSGSMGGnRFELAKEFVLKLVEQLdIGPDGdRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYKL-GGGT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553    119 YMHEGFERASEQIYYENRQGYRTA-SVIIALTDGElHEDLFFYSEREANRSRDLGAIVYCVGVK-DFNETQLARIADSKD 196
Cdd:smart00327  80 NLGAALQYALENLFSKSAGSRRGApKVVILITDGE-SNDGPKDLLKAAKELKRSGVKVFVVGVGnDVDEEELKKLASAPG 158

                          170
                   ....*....|....*..
gi 16933553    197 HVF-PVNDGFQALQGII 212
Cdd:smart00327 159 GVYvFLPELLDLLIDLL 175
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 44-199 1.46e-18

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: 81.46  E-value: 1.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  44 DLYFILDKSGSVLHH-WNEIYYFVEQLAHKFI--SPQLRMSFIVFSTRGTTLMKLTE--DREQIRQGLEELQKvLPGGDT 118
Cdd:cd00198   2 DIVFLLDVSGSMGGEkLDKAKEALKALVSSLSasPPGDRVGLVTFGSNARVVLPLTTdtDKADLLEAIDALKK-GLGGGT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 119 YMHEGFERASEQIYYENRQGYRtaSVIIALTDGELHEDLfFYSEREANRSRDLGAIVYCVGVKD-FNETQLARIAD--SK 195
Cdd:cd00198  81 NIGAALRLALELLKSAKRPNAR--RVIILLTDGEPNDGP-ELLAEAARELRKLGITVYTIGIGDdANEDELKEIADktTG 157


                ....
gi 16933553 196 DHVF 199
Cdd:cd00198 158 GAVF 161
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 44-180 9.10e-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: 79.74  E-value: 9.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  44 DLYFILDKSGSV-LHHWneiYYFVEQLAHKF-----ISPQ-LRMSFIVFSTRGTTLMKL----TEDREQIRQGLEELQKV 112
Cdd:cd01471   2 DLYLLVDGSGSIgYSNW---VTHVVPFLHTFvqnlnISPDeINLYLVTFSTNAKELIRLsspnSTNKDLALNAIRALLSL 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 113 -LPGGDTYMHEGFERAsEQIYYENRQGYRTA-SVIIALTDGElhEDLFFYSEREANRSRDLGAIVYCVGV 180
Cdd:cd01471  79 yYPNGSTNTTSALLVV-EKHLFDTRGNRENApQLVIIMTDGI--PDSKFRTLKEARKLRERGVIIAVLGV 145
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 42-215 2.88e-14

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 71.51  E-value: 2.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  42 GFDLYFILDKSGS--VLHHWNEIYYFVEQLAHKFiSPQLRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQkvlPGGDTY 119
Cdd:COG1240  92 GRDVVLVVDASGSmaAENRLEAAKGALLDFLDDY-RPRDRVGLVAFGGEAEVLLPLTRDREALKRALDELP---PGGGTP 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 120 MHEGFERASEQIYYENRQGYRtasVIIALTDGELH---EDLffysEREANRSRDLGAIVYCVGVKD--FNETQLARIADS 194
Cdd:COG1240 168 LGDALALALELLKRADPARRK---VIVLLTDGRDNagrIDP----LEAAELAAAAGIRIYTIGVGTeaVDEGLLREIAEA 240

                       170       180
                ....*....|....*....|..
gi 16933553 195 KD-HVFPVNDgFQALQGIIHSI 215
Cdd:COG1240 241 TGgRYFRADD-LSELAAIYREI 261
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 44-203 2.70e-13

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: 66.87  E-value: 2.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  44 DLYFILDKSGSV-LHHWNEIYYFVEQLAHKF-ISPQL-RMSFIVFSTRGTTLMKLTE--DREQIRQGLEELQkvLPGGDT 118
Cdd:cd01472   2 DIVFLVDGSESIgLSNFNLVKDFVKRVVERLdIGPDGvRVGVVQYSDDPRTEFYLNTyrSKDDVLEAVKNLR--YIGGGT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 119 YMHEGFERASEQIYYEN---RQGYRtaSVIIALTDGELHEDLffysEREANRSRDLGAIVYCVGVKDFNETQLARIADSK 195
Cdd:cd01472  80 NTGKALKYVRENLFTEAsgsREGVP--KVLVVITDGKSQDDV----EEPAVELKQAGIEVFAVGVKNADEEELKQIASDP 153

                       170
                ....*....|
gi 16933553 196 --DHVFPVND 203
Cdd:cd01472 154 keLYVFNVAD 163
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 44-199 1.33e-12

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 64.73  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  44 DLYFILDKSGSVLHHWN-EIYYFVEQLAHKFISPQ-LRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQKVLP--GGDTY 119
Cdd:cd01476   2 DLLFVLDSSGSVRGKFEkYKKYIERIVEGLEIGPTaTRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRfiGGTTA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 120 MHEGFERASEQIYYENRQGYRTASVIIALTDGELHEDlffyserEANRSRDL----GAIVYCVGVKD---FNETQLARIA 192
Cdd:cd01476  82 TGAAIEVALQQLDPSEGRREGIPKVVVVLTDGRSHDD-------PEKQARILravpNIETFAVGTGDpgtVDTEELHSIT 154


                ....*..
gi 16933553 193 DSKDHVF 199
Cdd:cd01476 155 GNEDHIF 161
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 44-193 8.22e-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: 64.74  E-value: 8.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  44 DLYFILDKSGSVlhHWNEIY-------YFVEQLahkfiSPQLRMSFIVFSTRGTTLMKLT--EDREQIRQGLEELQkvlP 114
Cdd:COG2304  93 NLVFVIDVSGSM--SGDKLElakeaakLLVDQL-----RPGDRVSIVTFAGDARVLLPPTpaTDRAKILAAIDRLQ---A 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 115 GGDTYMHEGFERASEQIyyENRQGYRTASVIIALTDGE------LHEDLffysEREANRSRDLGAIVYCVGV-KDFNETQ 187
Cdd:COG2304 163 GGGTALGAGLELAYELA--RKHFIPGRVNRVILLTDGDanvgitDPEEL----LKLAEEAREEGITLTTLGVgSDYNEDL 236


                ....*.
gi 16933553 188 LARIAD 193
Cdd:COG2304 237 LERLAD 242
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 44-203 2.97e-11

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: 61.15  E-value: 2.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  44 DLYFILDKSGSVLH-HWNEIYYFVEQLAHKF-ISPQ-LRMSFIVFSTRGTTLMKLTE--DREQIRQGLEELQkvLPGGDT 118
Cdd:cd01482   2 DIVFLVDGSWSIGRsNFNLVRSFLSSVVEAFeIGPDgVQVGLVQYSDDPRTEFDLNAytSKEDVLAAIKNLP--YKGGNT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 119 YMHEGFERASEQIYYEnRQGYRT--ASVIIALTDGELHEDLffysEREANRSRDLGAIVYCVGVKDFNETQLARIAD--S 194
Cdd:cd01482  80 RTGKALTHVREKNFTP-DAGARPgvPKVVILITDGKSQDDV----ELPARVLRNLGVNVFAVGVKDADESELKMIASkpS 154


                ....*....
gi 16933553 195 KDHVFPVND 203
Cdd:cd01482 155 ETHVFNVAD 163
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 44-193 6.09e-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: 58.92  E-value: 6.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  44 DLYFILDKSGSVlhhwneiYYFVEQLAhKFIS--------PQLRMSFIVFSTRGTTLMKLTEDREqIRQGLEELQKVLPG 115
Cdd:COG2425 120 PVVLCVDTSGSM-------AGSKEAAA-KAAAlallralrPNRRFGVILFDTEVVEDLPLTADDG-LEDAIEFLSGLFAG 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 116 GDTYMHEGFERASEQIyyeNRQGYRTASVIIaLTDGE---LHEDLFfyseREAnRSRDLGAIVYCVGVKDFNETQL-ARI 191
Cdd:COG2425 191 GGTDIAPALRAALELL---EEPDYRNADIVL-ITDGEagvSPEELL----REV-RAKESGVRLFTVAIGDAGNPGLlEAL 261


                ..
gi 16933553 192 AD 193
Cdd:COG2425 262 AD 263
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 44-211 2.20e-09

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 55.82  E-value: 2.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  44 DLYFILDKSGSVL-HHWNEIYYFVEQLAHKF--ISPQLRMSFIVFSTRGTTLMKLTE--DREQIRQGLEELQKVlpGGDT 118
Cdd:cd01469   2 DIVFVLDGSGSIYpDDFQKVKNFLSTVMKKLdiGPTKTQFGLVQYSESFRTEFTLNEyrTKEEPLSLVKHISQL--LGLT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 119 YMHEGFERASEQIYYENRQGYRTAS-VIIALTDGELHEDlffySEREA--NRSRDLGAIVYCVGVKDF--NET---QLAR 190
Cdd:cd01469  80 NTATAIQYVVTELFSESNGARKDATkVLVVITDGESHDD----PLLKDviPQAEREGIIRYAIGVGGHfqRENsreELKT 155

                       170       180
                ....*....|....*....|...
gi 16933553 191 IAD--SKDHVFPVNDgFQALQGI 211
Cdd:cd01469 156 IASkpPEEHFFNVTD-FAALKDI 177
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 44-192 1.73e-06

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: 47.77  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  44 DLYFILDKSGSV-LHHWNEIYYFVEQLAHKFISPQL--------RMSFIVFSTRGTT---LMKLTEDREQIRQGLEELQK 111
Cdd:cd01480   4 DITFVLDSSESVgLQNFDITKNFVKRVAERFLKDYYrkdpagswRVGVVQYSDQQEVeagFLRDIRNYTSLKEAVDNLEY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 112 VlpGGDTYMHEGFERASEQIYYENRQGyrTASVIIALTDGelHEDlffYS-----EREANRSRDLGAIVYCVGVKDFNET 186
Cdd:cd01480  84 I--GGGTFTDCALKYATEQLLEGSHQK--ENKFLLVITDG--HSD---GSpdggiEKAVNEADHLGIKIFFVAVGSQNEE 154


                ....*.
gi 16933553 187 QLARIA 192
Cdd:cd01480 155 PLSRIA 160
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
46-152 6.99e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 42.99  E-value: 6.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  46 YFILDKSGSV----LHHWNEIY-YFVEQL-AHKFISPQLRMSFIVFSTRGTTLMKLTeDREQIrqgleELQKVLPGGDTY 119
Cdd:COG4245   9 YLLLDTSGSMsgepIEALNEGLqALIDELrQDPYALETVEVSVITFDGEAKVLLPLT-DLEDF-----QPPDLSASGGTP 82

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16933553 120 MHEGFERASEQI------YYENRQGYRTASVIIaLTDGE 152
Cdd:COG4245  83 LGAALELLLDLIerrvqkYTAEGKGDWRPVVFL-ITDGE 120
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 42-180 1.85e-04

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: 41.55  E-value: 1.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  42 GFDLYFILDKSGSVL----HHWNEIYyFVEQLAHKFIS--PQLRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQKVLPG 115
Cdd:cd01467   2 GRDIMIALDVSGSMLaqdfVKPSRLE-AAKEVLSDFIDrrENDRIGLVVFAGAAFTQAPLTLDRESLKELLEDIKIGLAG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16933553 116 GDTYMHEGFERASEQIyyenRQGYRTASVIIALTDGELHEDlFFYSEREANRSRDLGAIVYCVGV 180
Cdd:cd01467  81 QGTAIGDAIGLAIKRL----KNSEAKERVIVLLTDGENNAG-EIDPATAAELAKNKGVRIYTIGV 140
VWA_2 pfam13519
von Willebrand factor type A domain;
45-146 3.77e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 39.20  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553    45 LYFILDKSGSV------LHHWNEIYYFVEQLAHKFisPQLRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQKVlpGGDT 118
Cdd:pfam13519   1 LVFVLDTSGSMrngdygPTRLEAAKDAVLALLKSL--PGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLEPK--GGGT 76

                          90       100
                  ....*....|....*....|....*...
gi 16933553   119 YMHEGFERASEQIyyENRQGYRTASVII 146
Cdd:pfam13519  77 NLAAALQLARAAL--KHRRKNQPRRIVL 102
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 45-199 6.68e-04

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: 39.95  E-value: 6.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553  45 LYFILDKSGSV----LHHWNE-IYYFVEQLahkfiSPQLRMSFIVFSTRGTTLMKLT--EDREQIRQGLEELQkvlPGGD 117
Cdd:cd01465   3 LVFVIDRSGSMdgpkLPLVKSaLKLLVDQL-----RPDDRLAIVTYDGAAETVLPATpvRDKAAILAAIDRLT---AGGS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16933553 118 TYMHEGFERASEQIyyenRQGYRTASV--IIALTDGELH--EDLFFYSEREANRSRDLGAIVYCVGV-KDFNETQLARIA 192
Cdd:cd01465  75 TAGGAGIQLGYQEA----QKHFVPGGVnrILLATDGDFNvgETDPDELARLVAQKRESGITLSTLGFgDNYNEDLMEAIA 150


                ....*..
gi 16933553 193 DSKDHVF 199
Cdd:cd01465 151 DAGNGNT 157
 
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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