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Conserved domains on  [gi|568989359|ref|XP_006519829|]
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uncharacterized protein LOC102631856 isoform X2 [Mus musculus]

Protein Classification

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 ...
 7-177 2.69e-33

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: 124.55  E-value: 2.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359   7 LYRSAHMLYGWPHVHKFVLDMVTRLSNPDLRVSIITYSCKGNVILPITGDREEILKGIERMKYSITAGHELIYQGLWKAN 86
Cdd:cd01474   11 LDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENAN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359  87 KQIIRGNRRGAQHPSMIIFLLHGPLDNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQIIGLAGGQEYAF-TNKKPEEL 165
Cdd:cd01474   91 EQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFpVTSGFQAL 170

                        170
                 ....*....|..
gi 568989359 166 SDLIIPLSSKAC 177
Cdd:cd01474  171 SGIIESVVKKAC 182
Anth_Ig super family cl05254
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 175-276 1.23e-18

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).


The actual alignment was detected with superfamily member pfam05587:

Pssm-ID: 461684  Cd Length: 102  Bit Score: 81.14  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359  175 KACPSLKTAITRIICIRESNPVLLEGYGFDFARRKEDVICRFYFGgaKKTIIDSPPINITKTTVTCPGPIVDSVGRAIHI 254
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTIN--ETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDV 78

                          90       100
                  ....*....|....*....|..
gi 568989359  255 QLSLDNGKNFLHNHLYVATRTC 276
Cdd:pfam05587  79 LVSLNNGKSFISSSLTITATTC 100
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 7-177 2.69e-33

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: 124.55  E-value: 2.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359   7 LYRSAHMLYGWPHVHKFVLDMVTRLSNPDLRVSIITYSCKGNVILPITGDREEILKGIERMKYSITAGHELIYQGLWKAN 86
Cdd:cd01474   11 LDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENAN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359  87 KQIIRGNRRGAQHPSMIIFLLHGPLDNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQIIGLAGGQEYAF-TNKKPEEL 165
Cdd:cd01474   91 EQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFpVTSGFQAL 170

                        170
                 ....*....|..
gi 568989359 166 SDLIIPLSSKAC 177
Cdd:cd01474  171 SGIIESVVKKAC 182
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 175-276 1.23e-18

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: 81.14  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359  175 KACPSLKTAITRIICIRESNPVLLEGYGFDFARRKEDVICRFYFGgaKKTIIDSPPINITKTTVTCPGPIVDSVGRAIHI 254
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTIN--ETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDV 78

                          90       100
                  ....*....|....*....|..
gi 568989359  255 QLSLDNGKNFLHNHLYVATRTC 276
Cdd:pfam05587  79 LVSLNNGKSFISSSLTITATTC 100
VWA pfam00092
von Willebrand factor type A domain;
15-169 2.44e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 47.65  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359   15 YGWPHVHKFVLDMVTRL--SNPDLRVSIITYSCKGNVILPIT--GDREEILKGIERMKYSiTAGHELIYQGLWKANKQII 90
Cdd:pfam00092  15 DNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNdySSKEELLSAVDNLRYL-GGGTTNTGKALKYALENLF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359   91 ---RGNRRGAqhPSMIIFLLHGpldNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQI--IGLAGGQEYAFTNKKPEEL 165
Cdd:pfam00092  94 ssaAGARPGA--PKVVVLLTDG---RSQDGDPEEVARELKSAGVTVFAVGVGNADDEELrkIASEPGEGHVFTVSDFEAL 168


                  ....
gi 568989359  166 SDLI 169
Cdd:pfam00092 169 EDLQ 172
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 7-177 2.69e-33

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: 124.55  E-value: 2.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359   7 LYRSAHMLYGWPHVHKFVLDMVTRLSNPDLRVSIITYSCKGNVILPITGDREEILKGIERMKYSITAGHELIYQGLWKAN 86
Cdd:cd01474   11 LDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHEGLENAN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359  87 KQIIRGNRRGAQHPSMIIFLLHGPLDNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQIIGLAGGQEYAF-TNKKPEEL 165
Cdd:cd01474   91 EQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYVFpVTSGFQAL 170

                        170
                 ....*....|..
gi 568989359 166 SDLIIPLSSKAC 177
Cdd:cd01474  171 SGIIESVVKKAC 182
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 175-276 1.23e-18

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: 81.14  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359  175 KACPSLKTAITRIICIRESNPVLLEGYGFDFARRKEDVICRFYFGgaKKTIIDSPPINITKTTVTCPGPIVDSVGRAIHI 254
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTIN--ETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDV 78

                          90       100
                  ....*....|....*....|..
gi 568989359  255 QLSLDNGKNFLHNHLYVATRTC 276
Cdd:pfam05587  79 LVSLNNGKSFISSSLTITATTC 100
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 15-151 3.49e-07

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: 49.98  E-value: 3.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359  15 YGWPHVHKFVLDMVTRLSNPDL--RVSIITYSCKGNVILPIT--GDREEILKGIERMKYsITAGHELIYQGLWKANKQII 90
Cdd:cd01450   16 ENFEKVKDFIEKLVEKLDIGPDktRVGLVQYSDDVRVEFSLNdyKSKDDLLKAVKNLKY-LGGGGTNTGKALQYALEQLF 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568989359  91 RGNRRGAQHPSMIIFLLHGPldNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQIIGLAG 151
Cdd:cd01450   95 SESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIAS 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-157 3.59e-07

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: 49.87  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359  17 WPHVHKFVLDMVTRLSN--PDLRVSIITYSCKGNVILPIT--GDREEILKGIERMKYSiTAGHELIYQGLWKANKQIIRG 92
Cdd:cd00198   18 LDKAKEALKALVSSLSAspPGDRVGLVTFGSNARVVLPLTtdTDKADLLEAIDALKKG-LGGGTNIGAALRLALELLKSA 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568989359  93 NRRGAqhPSMIIFLLHGpLDNQGYGYSLDETNDTRRMG--GYVCGVGTGQSERN-QIIGLAGGQEYAF 157
Cdd:cd00198   97 KRPNA--RRVIILLTDG-EPNDGPELLAEAARELRKLGitVYTIGIGDDANEDElKEIADKTTGGAVF 161
VWA pfam00092
von Willebrand factor type A domain;
15-169 2.44e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 47.65  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359   15 YGWPHVHKFVLDMVTRL--SNPDLRVSIITYSCKGNVILPIT--GDREEILKGIERMKYSiTAGHELIYQGLWKANKQII 90
Cdd:pfam00092  15 DNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNdySSKEELLSAVDNLRYL-GGGTTNTGKALKYALENLF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359   91 ---RGNRRGAqhPSMIIFLLHGpldNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQI--IGLAGGQEYAFTNKKPEEL 165
Cdd:pfam00092  94 ssaAGARPGA--PKVVVLLTDG---RSQDGDPEEVARELKSAGVTVFAVGVGNADDEELrkIASEPGEGHVFTVSDFEAL 168


                  ....
gi 568989359  166 SDLI 169
Cdd:pfam00092 169 EDLQ 172
VWA_2 pfam13519
von Willebrand factor type A domain;
9-106 1.19e-04

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 41.12  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359    9 RSAHMLYGWPHVHKF--VLDMVTRL--SNPDLRVSIITYSCKGNVILPITGDREEILKGIERMKysITAGHELIYQGLWK 84
Cdd:pfam13519   7 TSGSMRNGDYGPTRLeaAKDAVLALlkSLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLE--PKGGGTNLAAALQL 84

                          90       100
                  ....*....|....*....|..
gi 568989359   85 ANKQIirgNRRGAQHPSMIIFL 106
Cdd:pfam13519  85 ARAAL---KHRRKNQPRRIVLI 103
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 18-158 6.82e-03

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: 37.64  E-value: 6.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989359  18 PHVHKFVLDMVTRLsNPDLRVSIITYSCKGNVILPIT--GDREEILKGIERMKYS-ITAGHEliyqGLWKANKQIIRGNR 94
Cdd:cd01465   19 PLVKSALKLLVDQL-RPDDRLAIVTYDGAAETVLPATpvRDKAAILAAIDRLTAGgSTAGGA----GIQLGYQEAQKHFV 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568989359  95 RGAQHPsmiIFLL------HGPLDNQgygySLDETNDTRRMGG-YVCGVGTGQsERN----QIIGLAGGQEYAFT 158
Cdd:cd01465   94 PGGVNR---ILLAtdgdfnVGETDPD----ELARLVAQKRESGiTLSTLGFGD-NYNedlmEAIADAGNGNTAYI 160
 
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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