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Conserved domains on  [gi|52485853|ref|NP_001004439|]
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integrin alpha-11 precursor [Homo sapiens]

Protein Classification

integrin alpha( domain architecture ID 12192535)

integrin alpha forms a heterodimer with integrin beta to mediate cell-extracellular matrix and cell-cell interactions; integrin alpha is a component of integrin, a cell adhesion molecule that mediates cell-extracellular matrix and cell-cell interactions

Gene Ontology:  GO:0007155|GO:0008305|GO:0005178|GO:0046872
PubMed:  3028640|2199285|12297042|12826403|14689578|12361595|12234368

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 163-341 2.37e-92

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: 293.49  E-value: 2.37e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  163 MDIVIVLDGSNSIYP--WVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTeT 240
Cdd:cd01469    1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  241 RTAFGIEFARSEAF--QKGGRKGAKKVMIVITDGESHDSPDLEKVIQQSERDNVTRYAVAVLGYYNRrginpETFLNEIK 318
Cdd:cd01469   80 NTATAIQYVVTELFseSNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQR-----ENSREELK 154

                        170       180
                 ....*....|....*....|...
gi 52485853  319 YIASDPDDKHFFNVTDEAALKDI 341
Cdd:cd01469  155 TIASKPPEEHFFNVTDFAALKDI 177
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 636-1035 1.42e-29

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


The actual alignment was detected with superfamily member pfam08441:

Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 123.58  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    636 RPVVQINASLHFEPSKINIFHRDCKRSGRDATCLAAFLCFTpiFLAPHFQTTTVGIRYNATMD---ERRYTPRAH-LDEG 711
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFS--YTGKPIPNPSLVLNYELELDrqkKKGLPPRVLfLDSQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    712 GDRFTNRAVLLSSGQELCERINFHVLDTA-DYVKPVTFSVEYSLEDPDHG--------PMLDDGWPTTLRVSVPFWNGCN 782
Cdd:pfam08441   79 QPSLTGTLVLLSQGRKVCRTTKAYLRDEFrDKLSPIVISLNYSLRVDPRApsdlpglkPILDQNQPSTVQEQANFLKDCG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    783 EDEHCVPDLVLDARsdlptameYCQRVLRKPaqdcsaytlsfdttvfIIESTRQRVAVEATLENRGENAYSTVLNISQSA 862
Cdd:pfam08441  159 EDNVCVPDLQLSAK--------FDSRESDEP----------------LLLGDDNDLALEITVTNLGEDAYEAELYVTLPP 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    863 NLQFaSLIQKEDSDGSIEC----VNEERRLqkqVCNVSYPfFRAKAKVAFRLDFEFSK-SIFLHHLEIELAAGSDSNERD 937
Cdd:pfam08441  215 GLDY-SGVRREGSEKQLSCtakkENSTRQV---VCDLGNP-MKRGTQVTFGLRFSVSGlELSTEELSFDLQIRSTNEQNS 289

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    938 stkEDNVAPLRFHLKYEADVLFT---RSSSLSHYEVKPNSSLERY--DGIGPPFSCIFRIQNLGLFPIHGMMMKITIPIA 1012
Cdd:pfam08441  290 ---NSNPVSLKVPVVAEAQLSLSgvsKPDQVVGGSVKGESAMKPRseEDIGPLVEHTYEVINNGPSTVSGASLEISWPYE 366

                          410       420
                   ....*....|....*....|...
gi 52485853   1013 TRSGNRLLKLRDFLTDEaNTSCN 1035
Cdd:pfam08441  367 LSNGKWLLYLLDVQGQG-KGECS 388
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 538-592 4.48e-12

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 62.01  E-value: 4.48e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 52485853     538 QNARFGSSIASVRDLNQDSYNDVVVGAPLEDNHA--GAIYIFHGFRGSILKTPKQRI 592
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 476-518 1.18e-09

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 55.07  E-value: 1.18e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 52485853     476 IGSYFGSEITSV-DIDGDGVTDvLLVGAPMYfNEGRERGKVYVY 518
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRA-NDAGETGAVYVY 42
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 39-78 7.21e-05

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 41.59  E-value: 7.21e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 52485853      39 AFFGYTVQQH-DISGNK--WLVVGAPLEtNGYQKTGDVYKCPV 78
Cdd:smart00191    3 SYFGYSVAGVgDVNGDGypDLLVGAPRA-NDAGETGAVYVYFG 44
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 163-341 2.37e-92

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: 293.49  E-value: 2.37e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  163 MDIVIVLDGSNSIYP--WVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTeT 240
Cdd:cd01469    1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  241 RTAFGIEFARSEAF--QKGGRKGAKKVMIVITDGESHDSPDLEKVIQQSERDNVTRYAVAVLGYYNRrginpETFLNEIK 318
Cdd:cd01469   80 NTATAIQYVVTELFseSNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQR-----ENSREELK 154

                        170       180
                 ....*....|....*....|...
gi 52485853  319 YIASDPDDKHFFNVTDEAALKDI 341
Cdd:cd01469  155 TIASKPPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
164-344 8.57e-50

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 174.00  E-value: 8.57e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    164 DIVIVLDGSNSI--YPWVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETR 241
Cdd:pfam00092    1 DIVFLLDGSGSIggDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    242 TAFGIEFARSEAFQK--GGRKGAKKVMIVITDGESHDSpDLEKVIQQSERDNVTRYAVAVLGYYNRrginpetflnEIKY 319
Cdd:pfam00092   81 TGKALKYALENLFSSaaGARPGAPKVVVLLTDGRSQDG-DPEEVARELKSAGVTVFAVGVGNADDE----------ELRK 149

                          170       180
                   ....*....|....*....|....*
gi 52485853    320 IASDPDDKHFFNVTDEAALKDIVDA 344
Cdd:pfam00092  150 IASEPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 164-342 6.07e-38

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: 140.28  E-value: 6.07e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853     164 DIVIVLDGSNSIYP--WVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETR 241
Cdd:smart00327    1 DVVFLLDGSGSMGGnrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853     242 TAFGIEFARSEAF--QKGGRKGAKKVMIVITDGESHDSP-DLEKVIQQSERDNVTRYAVAVLGYYNRrginpetflNEIK 318
Cdd:smart00327   81 LGAALQYALENLFskSAGSRRGAPKVVILITDGESNDGPkDLLKAAKELKRSGVKVFVVGVGNDVDE---------EELK 151

                           170       180
                    ....*....|....*....|....
gi 52485853     319 YIASDPDDKHFFNVTDEAALKDIV 342
Cdd:smart00327  152 KLASAPGGVYVFLPELLDLLIDLL 175
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 636-1035 1.42e-29

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 123.58  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    636 RPVVQINASLHFEPSKINIFHRDCKRSGRDATCLAAFLCFTpiFLAPHFQTTTVGIRYNATMD---ERRYTPRAH-LDEG 711
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFS--YTGKPIPNPSLVLNYELELDrqkKKGLPPRVLfLDSQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    712 GDRFTNRAVLLSSGQELCERINFHVLDTA-DYVKPVTFSVEYSLEDPDHG--------PMLDDGWPTTLRVSVPFWNGCN 782
Cdd:pfam08441   79 QPSLTGTLVLLSQGRKVCRTTKAYLRDEFrDKLSPIVISLNYSLRVDPRApsdlpglkPILDQNQPSTVQEQANFLKDCG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    783 EDEHCVPDLVLDARsdlptameYCQRVLRKPaqdcsaytlsfdttvfIIESTRQRVAVEATLENRGENAYSTVLNISQSA 862
Cdd:pfam08441  159 EDNVCVPDLQLSAK--------FDSRESDEP----------------LLLGDDNDLALEITVTNLGEDAYEAELYVTLPP 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    863 NLQFaSLIQKEDSDGSIEC----VNEERRLqkqVCNVSYPfFRAKAKVAFRLDFEFSK-SIFLHHLEIELAAGSDSNERD 937
Cdd:pfam08441  215 GLDY-SGVRREGSEKQLSCtakkENSTRQV---VCDLGNP-MKRGTQVTFGLRFSVSGlELSTEELSFDLQIRSTNEQNS 289

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    938 stkEDNVAPLRFHLKYEADVLFT---RSSSLSHYEVKPNSSLERY--DGIGPPFSCIFRIQNLGLFPIHGMMMKITIPIA 1012
Cdd:pfam08441  290 ---NSNPVSLKVPVVAEAQLSLSgvsKPDQVVGGSVKGESAMKPRseEDIGPLVEHTYEVINNGPSTVSGASLEISWPYE 366

                          410       420
                   ....*....|....*....|...
gi 52485853   1013 TRSGNRLLKLRDFLTDEaNTSCN 1035
Cdd:pfam08441  367 LSNGKWLLYLLDVQGQG-KGECS 388
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 538-592 4.48e-12

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 62.01  E-value: 4.48e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 52485853     538 QNARFGSSIASVRDLNQDSYNDVVVGAPLEDNHA--GAIYIFHGFRGSILKTPKQRI 592
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 476-518 1.18e-09

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 55.07  E-value: 1.18e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 52485853     476 IGSYFGSEITSV-DIDGDGVTDvLLVGAPMYfNEGRERGKVYVY 518
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRA-NDAGETGAVYVY 42
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 151-346 5.36e-09

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: 58.41  E-value: 5.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  151 TVAPALQRCQTYMDIVIVLDGSNSIY---PWVEVQHFLINILKKFyigPGQIQVGVVQYGED--VVHEFhlndYRSVKDV 225
Cdd:COG1240   81 LAPLALARPQRGRDVVLVVDASGSMAaenRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEaeVLLPL----TRDREAL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  226 VEAASHIEQRGGTetRTAFGIEFARSEAfqKGGRKGAKKVMIVITDGESHDSP-DLEKVIQQSERDNVTRYAVavlgyyn 304
Cdd:COG1240  154 KRALDELPPGGGT--PLGDALALALELL--KRADPARRKVIVLLTDGRDNAGRiDPLEAAELAAAAGIRIYTI------- 222

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 52485853  305 rrGINPETF-LNEIKYIASDPDDKhFFNVTDEAALKDIVDALG 346
Cdd:COG1240  223 --GVGTEAVdEGLLREIAEATGGR-YFRADDLSELAAIYREID 262
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 542-577 2.43e-07

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 47.89  E-value: 2.43e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 52485853    542 FGSSIASVrDLNQDSYNDVVVGAPLEDN-HAGAIYIF 577
Cdd:pfam01839    1 FGYSVAVG-DLNGDGYADLAVGAPGEGGaGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 480-518 3.73e-07

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 47.51  E-value: 3.73e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 52485853    480 FGSEITSVDIDGDGVTDvLLVGAPMYFNEGreRGKVYVY 518
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAPGEGGAG--AGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 39-78 7.21e-05

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 41.59  E-value: 7.21e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 52485853      39 AFFGYTVQQH-DISGNK--WLVVGAPLEtNGYQKTGDVYKCPV 78
Cdd:smart00191    3 SYFGYSVAGVgDVNGDGypDLLVGAPRA-NDAGETGAVYVYFG 44
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 144-345 1.18e-04

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 45.38  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    144 SNFRFSKTVAPAlqrcqtymdIVIVLDGSNSIYPwveVQHFLINILKKF---YIGPgQIQVGVVQYGED--VVHEFH--- 215
Cdd:TIGR03436   44 ASFRRETDLPLT---------VGLVIDTSGSMRN---DLDRARAAAIRFlktVLRP-NDRVFVVTFNTRlrLLQDFTsdp 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    216 ------LNDYRSVKDVVEAASHIEQRGGTETRTAFGIEFArSEAFQKGGRKGA--KKVMIVITDGESHDS-PDLEKVIQQ 286
Cdd:TIGR03436  111 rlleaaLNRLKPPLRTDYNSSGAFVRDGGGTALYDAITLA-ALEQLANALAGIpgRKALIVISDGGDNRSrDTLERAIDA 189

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52485853    287 SERDNVTRYAV-------AVLGYYNRRGINPETFLNEIkyiaSDPDDKHFFnvtdEAALKDIVDAL 345
Cdd:TIGR03436  190 AQRADVAIYSIdarglraPDLGAGAKAGLGGPEALERL----AEETGGRAF----YVNSNDLDGAF 247
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 163-341 2.37e-92

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: 293.49  E-value: 2.37e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  163 MDIVIVLDGSNSIYP--WVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTeT 240
Cdd:cd01469    1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  241 RTAFGIEFARSEAF--QKGGRKGAKKVMIVITDGESHDSPDLEKVIQQSERDNVTRYAVAVLGYYNRrginpETFLNEIK 318
Cdd:cd01469   80 NTATAIQYVVTELFseSNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQR-----ENSREELK 154

                        170       180
                 ....*....|....*....|...
gi 52485853  319 YIASDPDDKHFFNVTDEAALKDI 341
Cdd:cd01469  155 TIASKPPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
164-344 8.57e-50

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 174.00  E-value: 8.57e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    164 DIVIVLDGSNSI--YPWVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETR 241
Cdd:pfam00092    1 DIVFLLDGSGSIggDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    242 TAFGIEFARSEAFQK--GGRKGAKKVMIVITDGESHDSpDLEKVIQQSERDNVTRYAVAVLGYYNRrginpetflnEIKY 319
Cdd:pfam00092   81 TGKALKYALENLFSSaaGARPGAPKVVVLLTDGRSQDG-DPEEVARELKSAGVTVFAVGVGNADDE----------ELRK 149

                          170       180
                   ....*....|....*....|....*
gi 52485853    320 IASDPDDKHFFNVTDEAALKDIVDA 344
Cdd:pfam00092  150 IASEPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 164-342 6.07e-38

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: 140.28  E-value: 6.07e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853     164 DIVIVLDGSNSIYP--WVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETR 241
Cdd:smart00327    1 DVVFLLDGSGSMGGnrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853     242 TAFGIEFARSEAF--QKGGRKGAKKVMIVITDGESHDSP-DLEKVIQQSERDNVTRYAVAVLGYYNRrginpetflNEIK 318
Cdd:smart00327   81 LGAALQYALENLFskSAGSRRGAPKVVILITDGESNDGPkDLLKAAKELKRSGVKVFVVGVGNDVDE---------EELK 151

                           170       180
                    ....*....|....*....|....
gi 52485853     319 YIASDPDDKHFFNVTDEAALKDIV 342
Cdd:smart00327  152 KLASAPGGVYVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 163-330 5.76e-37

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: 136.65  E-value: 5.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  163 MDIVIVLDGSNSIYP--WVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTET 240
Cdd:cd01450    1 LDIVFLLDGSESVGPenFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  241 RTAFGIEFARSEAFQKGG-RKGAKKVMIVITDGESHDSPDLEKVIQQSERDNVTRYAVAVLGYYNrrginpetflNEIKY 319
Cdd:cd01450   81 NTGKALQYALEQLFSESNaRENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADE----------EELRE 150

                        170
                 ....*....|.
gi 52485853  320 IASDPDDKHFF 330
Cdd:cd01450  151 IASCPSERHVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 164-334 1.70e-32

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: 123.94  E-value: 1.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  164 DIVIVLDGSNSI--YPWVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTeTR 241
Cdd:cd01482    2 DIVFLVDGSWSIgrSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGN-TR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  242 TAFGIEFARSEAF--QKGGRKGAKKVMIVITDGESHDspDLEKVIQQSERDNVTRYAVAVLgyynrrgiNPETflNEIKY 319
Cdd:cd01482   81 TGKALTHVREKNFtpDAGARPGVPKVVILITDGKSQD--DVELPARVLRNLGVNVFAVGVK--------DADE--SELKM 148

                        170
                 ....*....|....*
gi 52485853  320 IASDPDDKHFFNVTD 334
Cdd:cd01482  149 IASKPSETHVFNVAD 163
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 164-334 1.16e-30

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: 118.87  E-value: 1.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  164 DIVIVLDGSNSI--YPWVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTeTR 241
Cdd:cd01472    2 DIVFLVDGSESIglSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGG-TN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  242 TAFGIEFARSEAFQK--GGRKGAKKVMIVITDGESHDspDLEKVIQQSERDNVTRYAVAVlgyynrRGINPEtflnEIKY 319
Cdd:cd01472   81 TGKALKYVRENLFTEasGSREGVPKVLVVITDGKSQD--DVEEPAVELKQAGIEVFAVGV------KNADEE----ELKQ 148

                        170
                 ....*....|....*
gi 52485853  320 IASDPDDKHFFNVTD 334
Cdd:cd01472  149 IASDPKELYVFNVAD 163
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 636-1035 1.42e-29

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 123.58  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    636 RPVVQINASLHFEPSKINIFHRDCKRSGRDATCLAAFLCFTpiFLAPHFQTTTVGIRYNATMD---ERRYTPRAH-LDEG 711
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFS--YTGKPIPNPSLVLNYELELDrqkKKGLPPRVLfLDSQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    712 GDRFTNRAVLLSSGQELCERINFHVLDTA-DYVKPVTFSVEYSLEDPDHG--------PMLDDGWPTTLRVSVPFWNGCN 782
Cdd:pfam08441   79 QPSLTGTLVLLSQGRKVCRTTKAYLRDEFrDKLSPIVISLNYSLRVDPRApsdlpglkPILDQNQPSTVQEQANFLKDCG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    783 EDEHCVPDLVLDARsdlptameYCQRVLRKPaqdcsaytlsfdttvfIIESTRQRVAVEATLENRGENAYSTVLNISQSA 862
Cdd:pfam08441  159 EDNVCVPDLQLSAK--------FDSRESDEP----------------LLLGDDNDLALEITVTNLGEDAYEAELYVTLPP 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    863 NLQFaSLIQKEDSDGSIEC----VNEERRLqkqVCNVSYPfFRAKAKVAFRLDFEFSK-SIFLHHLEIELAAGSDSNERD 937
Cdd:pfam08441  215 GLDY-SGVRREGSEKQLSCtakkENSTRQV---VCDLGNP-MKRGTQVTFGLRFSVSGlELSTEELSFDLQIRSTNEQNS 289

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    938 stkEDNVAPLRFHLKYEADVLFT---RSSSLSHYEVKPNSSLERY--DGIGPPFSCIFRIQNLGLFPIHGMMMKITIPIA 1012
Cdd:pfam08441  290 ---NSNPVSLKVPVVAEAQLSLSgvsKPDQVVGGSVKGESAMKPRseEDIGPLVEHTYEVINNGPSTVSGASLEISWPYE 366

                          410       420
                   ....*....|....*....|...
gi 52485853   1013 TRSGNRLLKLRDFLTDEaNTSCN 1035
Cdd:pfam08441  367 LSNGKWLLYLLDVQGQG-KGECS 388
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 164-330 1.05e-26

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 107.27  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  164 DIVIVLDGSNSI--YPWVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETR 241
Cdd:cd00198    2 DIVFLLDVSGSMggEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  242 TAFGIEFARsEAFQKGGRKGAKKVMIVITDGESHDSP-DLEKVIQQSERDNVTRYAVAVLGYYNRRginpetflnEIKYI 320
Cdd:cd00198   82 IGAALRLAL-ELLKSAKRPNARRVIILLTDGEPNDGPeLLAEAARELRKLGITVYTIGIGDDANED---------ELKEI 151

                        170
                 ....*....|
gi 52485853  321 ASDPDDKHFF 330
Cdd:cd00198  152 ADKTTGGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 164-334 2.84e-22

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: 96.69  E-value: 2.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  164 DIVIVLDGSNSIYP--WVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRgGTETR 241
Cdd:cd01475    4 DLVFLIDSSRSVRPenFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGTM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  242 TAFGIEFARSEAFQ--KGGRKGAK---KVMIVITDGESHDspDLEKVIQQSERDNVTRYAVAVlgyynrrginPETFLNE 316
Cdd:cd01475   83 TGLAIQYAMNNAFSeaEGARPGSErvpRVGIVVTDGRPQD--DVSEVAAKARALGIEMFAVGV----------GRADEEE 150

                        170
                 ....*....|....*...
gi 52485853  317 IKYIASDPDDKHFFNVTD 334
Cdd:cd01475  151 LREIASEPLADHVFYVED 168
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 164-334 1.34e-17

VWA_collagen alpha 3(VI) like: 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: 238758  Cd Length: 165  Bit Score: 81.22  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  164 DIVIVLDGSNSIYPwVEVQH---FLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTET 240
Cdd:cd01481    2 DIVFLIDGSDNVGS-GNFPAirdFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  241 RTAFGIEFARSEAFQKGG----RKGAKKVMIVITDGESHDspDLEKVIQQSERDNVTRYAVAvlgyynRRGINPEtflnE 316
Cdd:cd01481   81 NTGSALDYVVKNLFTKSAgsriEEGVPQFLVLITGGKSQD--DVERPAVALKRAGIVPFAIG------ARNADLA----E 148

                        170
                 ....*....|....*...
gi 52485853  317 IKYIASDPDdkHFFNVTD 334
Cdd:cd01481  149 LQQIAFDPS--FVFQVSD 164
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 164-299 8.75e-14

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: 70.88  E-value: 8.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  164 DIVIVLDGSNSiypwVEVQHF---------LINILKKFY---IGPGQIQVGVVQYGEDVVHEF----HLNDYRSVKDVVE 227
Cdd:cd01480    4 DITFVLDSSES----VGLQNFditknfvkrVAERFLKDYyrkDPAGSWRVGVVQYSDQQEVEAgflrDIRNYTSLKEAVD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52485853  228 AASHIeqRGGTETRTAfgIEFARsEAFQKGGRKGAKKVMIVITDGESHDSPD--LEKVIQQSERDNVTRYAVAV 299
Cdd:cd01480   80 NLEYI--GGGTFTDCA--LKYAT-EQLLEGSHQKENKFLLVITDGHSDGSPDggIEKAVNEADHLGIKIFFVAV 148
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 164-278 2.09e-13

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: 69.35  E-value: 2.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  164 DIVIVLDGSNSIYPWVEVQ-HFLINILKKFYIGPGQIQVGVVQY-GEDVVH-EFHLNDYRSVKDVVEAASHIEQRGGTeT 240
Cdd:cd01476    2 DLLFVLDSSGSVRGKFEKYkKYIERIVEGLEIGPTATRVALITYsGRGRQRvRFNLPKHNDGEELLEKVDNLRFIGGT-T 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 52485853  241 RTAFGIEFArSEAFQK--GGRKGAKKVMIVITDGESHDSP 278
Cdd:cd01476   81 ATGAAIEVA-LQQLDPseGRREGIPKVVVVLTDGRSHDDP 119
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 159-345 3.66e-12

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: 66.38  E-value: 3.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  159 CQTYMDIVIVLDGSNSI-YPWVEVQHFLINILKKFyIGPGqIQVGVVQYGEDVVHEFHLNDYRsvKDVVEAASHIEQ-RG 236
Cdd:cd01474    1 CAGHFDLYFVLDKSGSVaANWIEIYDFVEQLVDRF-NSPG-LRFSFITFSTRATKILPLTDDS--SAIIKGLEVLKKvTP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  237 GTETRTAFGIEFARSEAFQK--GGRKGAKkVMIVITDGESHDSP--DLEKVIQQSERDNVTRYAVAVLGYYNRRGINpet 312
Cdd:cd01474   77 SGQTYIHEGLENANEQIFNRngGGRETVS-VIIALTDGQLLLNGhkYPEHEAKLSRKLGAIVYCVGVTDFLKSQLIN--- 152

                        170       180       190
                 ....*....|....*....|....*....|....
gi 52485853  313 flneikyIASDPDdkHFFNVTDE-AALKDIVDAL 345
Cdd:cd01474  153 -------IADSKE--YVFPVTSGfQALSGIIESV 177
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 538-592 4.48e-12

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 62.01  E-value: 4.48e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 52485853     538 QNARFGSSIASVRDLNQDSYNDVVVGAPLEDNHA--GAIYIFHGFRGSILKTPKQRI 592
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGGNSIPLQNL 57
VWA_2 pfam13519
von Willebrand factor type A domain;
165-269 1.11e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 62.31  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    165 IVIVLDGSNSIYP-------WVEVQHFLINILKKFyigPGQiQVGVVQYGEDVVHEFHLNDyrSVKDVVEAASHIEQRGG 237
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygptrLEAAKDAVLALLKSL---PGD-RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|..
gi 52485853    238 tETRTAFGIEFARSEAfqKGGRKGAKKVMIVI 269
Cdd:pfam13519   75 -GTNLAAALQLARAAL--KHRRKNQPRRIVLI 103
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 163-301 4.95e-11

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 63.17  E-value: 4.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  163 MDIVIVLDGSNSI--YPWV-EVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSV-KD----VVEAASHIEQ 234
Cdd:cd01471    1 LDLYLLVDGSGSIgySNWVtHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTnKDlalnAIRALLSLYY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52485853  235 RGGTeTRTAFGIEFARSEAF-QKGGRKGAKKVMIVITDGESHDSPDLEKVIQQSERDNVTryaVAVLG 301
Cdd:cd01471   81 PNGS-TNTTSALLVVEKHLFdTRGNRENAPQLVIIMTDGIPDSKFRTLKEARKLRERGVI---IAVLG 144
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 476-518 1.18e-09

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 55.07  E-value: 1.18e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 52485853     476 IGSYFGSEITSV-DIDGDGVTDvLLVGAPMYfNEGRERGKVYVY 518
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRA-NDAGETGAVYVY 42
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 151-346 5.36e-09

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: 58.41  E-value: 5.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  151 TVAPALQRCQTYMDIVIVLDGSNSIY---PWVEVQHFLINILKKFyigPGQIQVGVVQYGED--VVHEFhlndYRSVKDV 225
Cdd:COG1240   81 LAPLALARPQRGRDVVLVVDASGSMAaenRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEaeVLLPL----TRDREAL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  226 VEAASHIEQRGGTetRTAFGIEFARSEAfqKGGRKGAKKVMIVITDGESHDSP-DLEKVIQQSERDNVTRYAVavlgyyn 304
Cdd:COG1240  154 KRALDELPPGGGT--PLGDALALALELL--KRADPARRKVIVLLTDGRDNAGRiDPLEAAELAAAAGIRIYTI------- 222

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 52485853  305 rrGINPETF-LNEIKYIASDPDDKhFFNVTDEAALKDIVDALG 346
Cdd:COG1240  223 --GVGTEAVdEGLLREIAEATGGR-YFRADDLSELAAIYREID 262
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 542-577 2.43e-07

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 47.89  E-value: 2.43e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 52485853    542 FGSSIASVrDLNQDSYNDVVVGAPLEDN-HAGAIYIF 577
Cdd:pfam01839    1 FGYSVAVG-DLNGDGYADLAVGAPGEGGaGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 480-518 3.73e-07

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 47.51  E-value: 3.73e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 52485853    480 FGSEITSVDIDGDGVTDvLLVGAPMYFNEGreRGKVYVY 518
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAPGEGGAG--AGAVYVL 36
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 164-308 6.28e-07

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 52.37  E-value: 6.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  164 DIVIVLDGSNSIYPWVEVQ-----HFLINILKKfyigpgQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGT 238
Cdd:COG2425  120 PVVLCVDTSGSMAGSKEAAakaaaLALLRALRP------NRRFGVILFDTEVVEDLPLTADDGLEDAIEFLSGLFAGGGT 193

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52485853  239 EtrtafgIEFARSEAFQK-GGRKGAKKVMIVITDGESHDSPD--LEKVIQQseRDNVTRYAVAvLGYYNRRGI 308
Cdd:COG2425  194 D------IAPALRAALELlEEPDYRNADIVLITDGEAGVSPEelLREVRAK--ESGVRLFTVA-IGDAGNPGL 257
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 163-343 2.93e-05

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: 46.13  E-value: 2.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  163 MDIVIVLDGSNSIYPwvevQHF---------LINILKKFYIGPgqiQVGVVQYGEDV-----VHEFHLNDYRSVKDVVEA 228
Cdd:cd01470    1 LNIYIALDASDSIGE----EDFdeaknaiktLIEKISSYEVSP---RYEIISYASDPkeivsIRDFNSNDADDVIKRLED 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853  229 ASH--IEQRGGTETRTAFGIEFARSEAFQKGGRKGAKK---VMIVITDGESHDSPDLEKVIQQSeRDNVtryavavlgYY 303
Cdd:cd01470   74 FNYddHGDKTGTNTAAALKKVYERMALEKVRNKEAFNEtrhVIILFTDGKSNMGGSPLPTVDKI-KNLV---------YK 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 52485853  304 NRR--------------GINPETFLNEIKYIASD-PDDKHFFNVTDEAALKDIVD 343
Cdd:cd01470  144 NNKsdnpredyldvyvfGVGDDVNKEELNDLASKkDNERHFFKLKDYEDLQEVFD 198
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 39-78 7.21e-05

Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate cell-extracellular matrix and cell-cell interactions. They contain both alpha and beta subunits. Alpha integrins are proposed to contain a domain containing a 7-fold repeat that adopts a beta-propellor fold. Some of these domains contain an inserted von Willebrand factor type-A domain. Some repeats contain putative calcium-binding sites. The 7-fold repeat domain is homologous to a similar domain in phosphatidylinositol-glycan-specific phospholipase D.


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 41.59  E-value: 7.21e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 52485853      39 AFFGYTVQQH-DISGNK--WLVVGAPLEtNGYQKTGDVYKCPV 78
Cdd:smart00191    3 SYFGYSVAGVgDVNGDGypDLLVGAPRA-NDAGETGAVYVYFG 44
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 144-345 1.18e-04

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 45.38  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    144 SNFRFSKTVAPAlqrcqtymdIVIVLDGSNSIYPwveVQHFLINILKKF---YIGPgQIQVGVVQYGED--VVHEFH--- 215
Cdd:TIGR03436   44 ASFRRETDLPLT---------VGLVIDTSGSMRN---DLDRARAAAIRFlktVLRP-NDRVFVVTFNTRlrLLQDFTsdp 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52485853    216 ------LNDYRSVKDVVEAASHIEQRGGTETRTAFGIEFArSEAFQKGGRKGA--KKVMIVITDGESHDS-PDLEKVIQQ 286
Cdd:TIGR03436  111 rlleaaLNRLKPPLRTDYNSSGAFVRDGGGTALYDAITLA-ALEQLANALAGIpgRKALIVISDGGDNRSrDTLERAIDA 189

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52485853    287 SERDNVTRYAV-------AVLGYYNRRGINPETFLNEIkyiaSDPDDKHFFnvtdEAALKDIVDAL 345
Cdd:TIGR03436  190 AQRADVAIYSIdarglraPDLGAGAKAGLGGPEALERL----AEETGGRAF----YVNSNDLDGAF 247
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 488-562 2.25e-04

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 40.29  E-value: 2.25e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52485853    488 DIDGDGVTDVLLVGapmyfnegreRGKVYVYELRQnlfvyNGTLKDSHSYQNARFGSSIA-SVRDLNQDSYNDVVV 562
Cdd:pfam13517    1 DLDGDGKLDLVVAN----------DGGLRLYLNNG-----DGTFTFITSVSLGGGGGGLSvAVGDLDGDGRLDLLV 61
 
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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