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Conserved domains on  [gi|41054731|ref|NP_032422|]
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integrin alpha-2 precursor [Mus musculus]

Protein Classification

integrin alpha( domain architecture ID 12192537)

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

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 ...
 170-350 7.29e-77

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: 250.74  E-value: 7.29e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  170 VDVVVVCDESNSIYP--WEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGdLT 247
Cdd:cd01469    1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  248 NTFRAIEFARDYAYSQTSGGRPGATKVMVVVTDGESHDGSKLKTVIQQCNDDEILRFGIAVLGYLNRnaldtKNLIKEIK 327
Cdd:cd01469   80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQR-----ENSREELK 154

                        170       180
                 ....*....|....*....|...
gi 41054731  328 AIASTPTERYFFNVADEAALLEK 350
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 ...
 672-1057 5.81e-45

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: 169.42  E-value: 5.81e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    672 ITLKLCFRAEFRPAgQNNQVAILFNMTLDADGHSSRVtSRGVFRENSERFLQKNMVVNEVQK--CSEHHISIQKPS-DVV 748
Cdd:pfam08441   34 FTVRACFSYTGKPI-PNPSLVLNYELELDRQKKKGLP-PRVLFLDSQQPSLTGTLVLLSQGRkvCRTTKAYLRDEFrDKL 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    749 NPLDLRVDISLENPGTS--------PALEAYSETVKVFSIPFYKECGSDGICISDLILDVQQLPAIQTQSFIVSNQNK-R 819
Cdd:pfam08441  112 SPIVISLNYSLRVDPRApsdlpglkPILDQNQPSTVQEQANFLKDCGEDNVCVPDLQLSAKFDSRESDEPLLLGDDNDlA 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    820 LTFSVilKNRGESAYNTVVLAEFSENLFFASFSMPVDGTEVTCEVGSSQKSVT--CDVGYPaLKSEQQVTFTINFDF-NL 896
Cdd:pfam08441  192 LEITV--TNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENSTRQvvCDLGNP-MKRGTQVTFGLRFSVsGL 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    897 QNLQNQAAINFQAFSESQETNKaDNSVSLTIPLLYDAELHLT-RSTNINFYEISSDENAPSVIKSVEDIGPK--FIFSLK 973
Cdd:pfam08441  269 ELSTEELSFDLQIRSTNEQNSN-SNPVSLKVPVVAEAQLSLSgVSKPDQVVGGSVKGESAMKPRSEEDIGPLveHTYEVI 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    974 VTaGSAPVSMALVTIHIPQYTKEKNPLLYLTGIQTDqaGDISCTA--EINPLKL----PHTAPSVSF------------- 1034
Cdd:pfam08441  348 NN-GPSTVSGASLEISWPYELSNGKWLLYLLDVQGQ--GKGECSPqnEINPLNLtqslESSKPLRTSrvhhvvkrrdvlk 424

                          410       420
                   ....*....|....*....|....*
gi 41054731   1035 -KNENFRHTKELDC-RTTSCSNITC 1057
Cdd:pfam08441  425 sEKATQTASVLLSCdSGARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 548-601 3.09e-13

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: 65.47  E-value: 3.09e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 41054731     548 NARFGSAIAALSDINMDGFNDVIVGSPVENENS--GAVYIYNGHQGTIRTKYSQKI 601
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 484-532 5.43e-07

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: 47.76  E-value: 5.43e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 41054731     484 IGSYFGSVLCSV-DVDKDTITDvLLVGAPTYMNDlkKEEGKVYLFTITKG 532
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRANDA--GETGAVYVYFGSSG 47
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 611-637 4.03e-04

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: 39.67  E-value: 4.03e-04
                            10        20
                    ....*....|....*....|....*..
gi 41054731     611 HLQFFGRSLDGYGDLNGDSITDVSIGA 637
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGA 27
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 44-92 4.81e-04

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: 39.28  E-value: 4.81e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 41054731      44 QFGYSVQQLTNPQGN---WLLVGSPWSGfPENRMGDVYKCPVDLPTATCEKL 92
Cdd:smart00191    4 YFGYSVAGVGDVNGDgypDLLVGAPRAN-DAGETGAVYVYFGSSGGGNSIPL 54
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 430-473 9.78e-04

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: 38.51  E-value: 9.78e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 41054731     430 HSSFLGYSVAAISTEDG---VHFVAGAPRAN---YTGQIVLYSVNKQGNV 473
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGdgyPDLLVGAPRANdagETGAVYVYFGSSGGGN 50
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1152-1166 1.68e-03

Integrin alpha cytoplasmic region; This family contains the short intracellular region of integrin alpha chains.


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.71  E-value: 1.68e-03
                           10
                   ....*....|....*
gi 41054731   1152 KLGFFKRQYKKMGQN 1166
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
 
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 ...
 170-350 7.29e-77

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: 250.74  E-value: 7.29e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  170 VDVVVVCDESNSIYP--WEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGdLT 247
Cdd:cd01469    1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  248 NTFRAIEFARDYAYSQTSGGRPGATKVMVVVTDGESHDGSKLKTVIQQCNDDEILRFGIAVLGYLNRnaldtKNLIKEIK 327
Cdd:cd01469   80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQR-----ENSREELK 154

                        170       180
                 ....*....|....*....|...
gi 41054731  328 AIASTPTERYFFNVADEAALLEK 350
Cdd:cd01469  155 TIASKPPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
171-349 2.44e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 167.07  E-value: 2.44e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    171 DVVVVCDESNSI--YPWEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGDLTN 248
Cdd:pfam00092    1 DIVFLLDGSGSIggDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    249 TFRAIEFARDYAYSQTSGGRPGATKVMVVVTDGESHDGSkLKTVIQQCNDDEILRFGIAVlgylnrnaldTKNLIKEIKA 328
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGD-PEEVARELKSAGVTVFAVGV----------GNADDEELRK 149

                          170       180
                   ....*....|....*....|.
gi 41054731    329 IASTPTERYFFNVADEAALLE 349
Cdd:pfam00092  150 IASEPGEGHVFTVSDFEALED 170
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 672-1057 5.81e-45

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: 169.42  E-value: 5.81e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    672 ITLKLCFRAEFRPAgQNNQVAILFNMTLDADGHSSRVtSRGVFRENSERFLQKNMVVNEVQK--CSEHHISIQKPS-DVV 748
Cdd:pfam08441   34 FTVRACFSYTGKPI-PNPSLVLNYELELDRQKKKGLP-PRVLFLDSQQPSLTGTLVLLSQGRkvCRTTKAYLRDEFrDKL 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    749 NPLDLRVDISLENPGTS--------PALEAYSETVKVFSIPFYKECGSDGICISDLILDVQQLPAIQTQSFIVSNQNK-R 819
Cdd:pfam08441  112 SPIVISLNYSLRVDPRApsdlpglkPILDQNQPSTVQEQANFLKDCGEDNVCVPDLQLSAKFDSRESDEPLLLGDDNDlA 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    820 LTFSVilKNRGESAYNTVVLAEFSENLFFASFSMPVDGTEVTCEVGSSQKSVT--CDVGYPaLKSEQQVTFTINFDF-NL 896
Cdd:pfam08441  192 LEITV--TNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENSTRQvvCDLGNP-MKRGTQVTFGLRFSVsGL 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    897 QNLQNQAAINFQAFSESQETNKaDNSVSLTIPLLYDAELHLT-RSTNINFYEISSDENAPSVIKSVEDIGPK--FIFSLK 973
Cdd:pfam08441  269 ELSTEELSFDLQIRSTNEQNSN-SNPVSLKVPVVAEAQLSLSgVSKPDQVVGGSVKGESAMKPRSEEDIGPLveHTYEVI 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    974 VTaGSAPVSMALVTIHIPQYTKEKNPLLYLTGIQTDqaGDISCTA--EINPLKL----PHTAPSVSF------------- 1034
Cdd:pfam08441  348 NN-GPSTVSGASLEISWPYELSNGKWLLYLLDVQGQ--GKGECSPqnEINPLNLtqslESSKPLRTSrvhhvvkrrdvlk 424

                          410       420
                   ....*....|....*....|....*
gi 41054731   1035 -KNENFRHTKELDC-RTTSCSNITC 1057
Cdd:pfam08441  425 sEKATQTASVLLSCdSGARCVVIRC 449
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 171-349 2.24e-39

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: 144.13  E-value: 2.24e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731     171 DVVVVCDESNSIYP--WEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGDLTN 248
Cdd:smart00327    1 DVVFLLDGSGSMGGnrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731     249 TFRAIEFARDYAYSQTSGGRPGATKVMVVVTDGESHDGSK-LKTVIQQCNDDEILRFGIAVLGYLNRNaldtknlikEIK 327
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDEE---------ELK 151

                           170       180
                    ....*....|....*....|..
gi 41054731     328 AIASTPTERYFFNVADEAALLE 349
Cdd:smart00327  152 KLASAPGGVYVFLPELLDLLID 173
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 548-601 3.09e-13

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: 65.47  E-value: 3.09e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 41054731     548 NARFGSAIAALSDINMDGFNDVIVGSPVENENS--GAVYIYNGHQGTIRTKYSQKI 601
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGGNSIPLQNL 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 148-347 1.49e-07

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: 54.17  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  148 DVSPDFQFLTSFSPAVQACPSLVDVVVVCDESNSIY---PWEAVKNFLVKFVTGLdigPKKTQVALIQYANEPRIIFNL- 223
Cdd:COG1240   71 AVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAaenRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLt 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  224 NDFETKEDMVQATSetrqhGGDLTNTFRAIEfardYAYSQTSGGRPGATKVMVVVTDGESHDGSK-LKTVIQQCNDDEIl 302
Cdd:COG1240  148 RDREALKRALDELP-----PGGGTPLGDALA----LALELLKRADPARRKVIVLLTDGRDNAGRIdPLEAAELAAAAGI- 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 41054731  303 rfGIAVLGYlNRNALDTKNLikeiKAIASTpTERYFFNVADEAAL 347
Cdd:COG1240  218 --RIYTIGV-GTEAVDEGLL----REIAEA-TGGRYFRADDLSEL 254
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 484-532 5.43e-07

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: 47.76  E-value: 5.43e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 41054731     484 IGSYFGSVLCSV-DVDKDTITDvLLVGAPTYMNDlkKEEGKVYLFTITKG 532
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRANDA--GETGAVYVYFGSSG 47
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 551-586 1.13e-06

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: 45.96  E-value: 1.13e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 41054731    551 FGSAIAALsDINMDGFNDVIVGSPVENE-NSGAVYIY 586
Cdd:pfam01839    1 FGYSVAVG-DLNGDGYADLAVGAPGEGGaGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 611-637 4.03e-04

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: 39.67  E-value: 4.03e-04
                            10        20
                    ....*....|....*....|....*..
gi 41054731     611 HLQFFGRSLDGYGDLNGDSITDVSIGA 637
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGA 27
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 44-92 4.81e-04

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: 39.28  E-value: 4.81e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 41054731      44 QFGYSVQQLTNPQGN---WLLVGSPWSGfPENRMGDVYKCPVDLPTATCEKL 92
Cdd:smart00191    4 YFGYSVAGVGDVNGDgypDLLVGAPRAN-DAGETGAVYVYFGSSGGGNSIPL 54
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 430-473 9.78e-04

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: 38.51  E-value: 9.78e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 41054731     430 HSSFLGYSVAAISTEDG---VHFVAGAPRAN---YTGQIVLYSVNKQGNV 473
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGdgyPDLLVGAPRANdagETGAVYVYFGSSGGGN 50
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 488-527 1.64e-03

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: 37.10  E-value: 1.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 41054731    488 FGSVLCSVDVDKDTITDvLLVGAPTYMNDlkkEEGKVYLF 527
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAPGEGGA---GAGAVYVL 36
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1152-1166 1.68e-03

Integrin alpha cytoplasmic region; This family contains the short intracellular region of integrin alpha chains.


Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.71  E-value: 1.68e-03
                           10
                   ....*....|....*
gi 41054731   1152 KLGFFKRQYKKMGQN 1166
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
 
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 ...
 170-350 7.29e-77

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: 250.74  E-value: 7.29e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  170 VDVVVVCDESNSIYP--WEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGdLT 247
Cdd:cd01469    1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLG-LT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  248 NTFRAIEFARDYAYSQTSGGRPGATKVMVVVTDGESHDGSKLKTVIQQCNDDEILRFGIAVLGYLNRnaldtKNLIKEIK 327
Cdd:cd01469   80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQR-----ENSREELK 154

                        170       180
                 ....*....|....*....|...
gi 41054731  328 AIASTPTERYFFNVADEAALLEK 350
Cdd:cd01469  155 TIASKPPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
171-349 2.44e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 167.07  E-value: 2.44e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    171 DVVVVCDESNSI--YPWEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGDLTN 248
Cdd:pfam00092    1 DIVFLLDGSGSIggDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    249 TFRAIEFARDYAYSQTSGGRPGATKVMVVVTDGESHDGSkLKTVIQQCNDDEILRFGIAVlgylnrnaldTKNLIKEIKA 328
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGD-PEEVARELKSAGVTVFAVGV----------GNADDEELRK 149

                          170       180
                   ....*....|....*....|.
gi 41054731    329 IASTPTERYFFNVADEAALLE 349
Cdd:pfam00092  150 IASEPGEGHVFTVSDFEALED 170
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 672-1057 5.81e-45

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: 169.42  E-value: 5.81e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    672 ITLKLCFRAEFRPAgQNNQVAILFNMTLDADGHSSRVtSRGVFRENSERFLQKNMVVNEVQK--CSEHHISIQKPS-DVV 748
Cdd:pfam08441   34 FTVRACFSYTGKPI-PNPSLVLNYELELDRQKKKGLP-PRVLFLDSQQPSLTGTLVLLSQGRkvCRTTKAYLRDEFrDKL 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    749 NPLDLRVDISLENPGTS--------PALEAYSETVKVFSIPFYKECGSDGICISDLILDVQQLPAIQTQSFIVSNQNK-R 819
Cdd:pfam08441  112 SPIVISLNYSLRVDPRApsdlpglkPILDQNQPSTVQEQANFLKDCGEDNVCVPDLQLSAKFDSRESDEPLLLGDDNDlA 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    820 LTFSVilKNRGESAYNTVVLAEFSENLFFASFSMPVDGTEVTCEVGSSQKSVT--CDVGYPaLKSEQQVTFTINFDF-NL 896
Cdd:pfam08441  192 LEITV--TNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENSTRQvvCDLGNP-MKRGTQVTFGLRFSVsGL 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    897 QNLQNQAAINFQAFSESQETNKaDNSVSLTIPLLYDAELHLT-RSTNINFYEISSDENAPSVIKSVEDIGPK--FIFSLK 973
Cdd:pfam08441  269 ELSTEELSFDLQIRSTNEQNSN-SNPVSLKVPVVAEAQLSLSgVSKPDQVVGGSVKGESAMKPRSEEDIGPLveHTYEVI 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    974 VTaGSAPVSMALVTIHIPQYTKEKNPLLYLTGIQTDqaGDISCTA--EINPLKL----PHTAPSVSF------------- 1034
Cdd:pfam08441  348 NN-GPSTVSGASLEISWPYELSNGKWLLYLLDVQGQ--GKGECSPqnEINPLNLtqslESSKPLRTSrvhhvvkrrdvlk 424

                          410       420
                   ....*....|....*....|....*
gi 41054731   1035 -KNENFRHTKELDC-RTTSCSNITC 1057
Cdd:pfam08441  425 sEKATQTASVLLSCdSGARCVVIRC 449
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 171-349 2.24e-39

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: 144.13  E-value: 2.24e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731     171 DVVVVCDESNSIYP--WEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGDLTN 248
Cdd:smart00327    1 DVVFLLDGSGSMGGnrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731     249 TFRAIEFARDYAYSQTSGGRPGATKVMVVVTDGESHDGSK-LKTVIQQCNDDEILRFGIAVLGYLNRNaldtknlikEIK 327
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdLLKAAKELKRSGVKVFVVGVGNDVDEE---------ELK 151

                           170       180
                    ....*....|....*....|..
gi 41054731     328 AIASTPTERYFFNVADEAALLE 349
Cdd:smart00327  152 KLASAPGGVYVFLPELLDLLID 173
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 170-339 7.84e-39

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: 142.05  E-value: 7.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  170 VDVVVVCDESNSIYP--WEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGDLT 247
Cdd:cd01450    1 LDIVFLLDGSESVGPenFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  248 NTFRAIEFARDYaYSQTSGGRPGATKVMVVVTDGESHDGSKLKTVIQQCNDDEILRFGIAVLGYLNrnaldtknliKEIK 327
Cdd:cd01450   81 NTGKALQYALEQ-LFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADE----------EELR 149

                        170
                 ....*....|..
gi 41054731  328 AIASTPTERYFF 339
Cdd:cd01450  150 EIASCPSERHVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 171-343 4.52e-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: 122.78  E-value: 4.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  171 DVVVVCDESNSI--YPWEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGdLTN 248
Cdd:cd01482    2 DIVFLVDGSWSIgrSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG-NTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  249 TFRAIEFARDYAYSQTSGGRPGATKVMVVVTDGESHDGSKLKTviqqcndDEILRFGIAVLgylnrnALDTKNLI-KEIK 327
Cdd:cd01482   81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPA-------RVLRNLGVNVF------AVGVKDADeSELK 147

                        170
                 ....*....|....*.
gi 41054731  328 AIASTPTERYFFNVAD 343
Cdd:cd01482  148 MIASKPSETHVFNVAD 163
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 170-343 9.45e-32

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: 121.95  E-value: 9.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  170 VDVVVVCDESNSI--YPWEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGdLT 247
Cdd:cd01472    1 ADIVFLVDGSESIglSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG-GT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  248 NTFRAIEFARDYAYSQTSGGRPGATKVMVVVTDGESHDGSKLKTViqqcnddEILRFGIAVLGYLNRNALDTknlikEIK 327
Cdd:cd01472   80 NTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAV-------ELKQAGIEVFAVGVKNADEE-----ELK 147

                        170
                 ....*....|....*.
gi 41054731  328 AIASTPTERYFFNVAD 343
Cdd:cd01472  148 QIASDPKELYVFNVAD 163
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 170-343 4.36e-26

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: 107.86  E-value: 4.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  170 VDVVVVCDESNSIYP--WEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETrQHGGDLT 247
Cdd:cd01475    3 TDLVFLIDSSRSVRPenFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRM-EYLETGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  248 NTFRAIEFARDYAYSQTSGGRPGAT---KVMVVVTDGESHDgsKLKTVIQQCNDDEILRFGIAVlgylnrnaldTKNLIK 324
Cdd:cd01475   82 MTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQD--DVSEVAAKARALGIEMFAVGV----------GRADEE 149

                        170
                 ....*....|....*....
gi 41054731  325 EIKAIASTPTERYFFNVAD 343
Cdd:cd01475  150 ELREIASEPLADHVFYVED 168
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 170-339 2.68e-23

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: 97.64  E-value: 2.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  170 VDVVVVCDESNSI--YPWEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGDLT 247
Cdd:cd00198    1 ADIVFLLDVSGSMggEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  248 NTFRAIEFARDYAYSQTsggRPGATKVMVVVTDGESHDG-SKLKTVIQQCNDDEILRFGIAVlgylnrnalDTKNLIKEI 326
Cdd:cd00198   81 NIGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGpELLAEAARELRKLGITVYTIGI---------GDDANEDEL 148

                        170
                 ....*....|...
gi 41054731  327 KAIASTPTERYFF 339
Cdd:cd00198  149 KEIADKTTGGAVF 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 171-288 2.26e-22

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: 95.16  E-value: 2.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  171 DVVVVCDESNSIYP-WEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPR--IIFNLNDFETKEDMVQATSETRQHGGdLT 247
Cdd:cd01476    2 DLLFVLDSSGSVRGkFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGG-TT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 41054731  248 NTFRAIEFARDYaYSQTSGGRPGATKVMVVVTDGESHDGSK 288
Cdd:cd01476   81 ATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDDPE 120
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 171-343 3.59e-20

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: 88.92  E-value: 3.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  171 DVVVVCDESNSIYP--WEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGDLTN 248
Cdd:cd01481    2 DIVFLIDGSDNVGSgnFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  249 TFRAIEFARDYAYSQTSGGR--PGATKVMVVVTDGESHDgsklkTVIQQCNddEILRFGIAVLGYLNRNALDTknlikEI 326
Cdd:cd01481   82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQD-----DVERPAV--ALKRAGIVPFAIGARNADLA-----EL 149

                        170
                 ....*....|....*..
gi 41054731  327 KAIASTPteRYFFNVAD 343
Cdd:cd01481  150 QQIAFDP--SFVFQVSD 164
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 548-601 3.09e-13

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: 65.47  E-value: 3.09e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 41054731     548 NARFGSAIAALSDINMDGFNDVIVGSPVENENS--GAVYIYNGHQGTIRTKYSQKI 601
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGGNSIPLQNL 57
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 170-285 6.94e-09

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: 56.62  E-value: 6.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  170 VDVVVVCDESNSI--YPW-EAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDF-----ETKEDMVQATSETRQ 241
Cdd:cd01471    1 LDLYLLVDGSGSIgySNWvTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPnstnkDLALNAIRALLSLYY 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 41054731  242 HGGDlTNTFRAIEFARDYAYSqTSGGRPGATKVMVVVTDGESHD 285
Cdd:cd01471   81 PNGS-TNTTSALLVVEKHLFD-TRGNRENAPQLVIIMTDGIPDS 122
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 166-292 5.07e-08

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: 54.31  E-value: 5.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  166 CPslVDVVVVCDESNSI--YPWEAVKNFLVKFV------TGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATS 237
Cdd:cd01480    1 GP--VDITFVLDSSESVglQNFDITKNFVKRVAerflkdYYRKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41054731  238 ETRQHGGDLTNTFRAIEFARDYaYSQTSGGrpGATKVMVVVTDGESH---DGSKLKTV 292
Cdd:cd01480   79 DNLEYIGGGTFTDCALKYATEQ-LLEGSHQ--KENKFLLVITDGHSDgspDGGIEKAV 133
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 148-347 1.49e-07

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: 54.17  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  148 DVSPDFQFLTSFSPAVQACPSLVDVVVVCDESNSIY---PWEAVKNFLVKFVTGLdigPKKTQVALIQYANEPRIIFNL- 223
Cdd:COG1240   71 AVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAaenRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLt 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  224 NDFETKEDMVQATSetrqhGGDLTNTFRAIEfardYAYSQTSGGRPGATKVMVVVTDGESHDGSK-LKTVIQQCNDDEIl 302
Cdd:COG1240  148 RDREALKRALDELP-----PGGGTPLGDALA----LALELLKRADPARRKVIVLLTDGRDNAGRIdPLEAAELAAAAGI- 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 41054731  303 rfGIAVLGYlNRNALDTKNLikeiKAIASTpTERYFFNVADEAAL 347
Cdd:COG1240  218 --RIYTIGV-GTEAVDEGLL----REIAEA-TGGRYFRADDLSEL 254
VWA_2 pfam13519
von Willebrand factor type A domain;
172-278 1.83e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 50.37  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731    172 VVVVCDESNSIYP-------WEAVKNFLVKFVTGLDIgpkkTQVALIQYANEPRIIFNLNDfeTKEDMVQATSETRQHGG 244
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygptrLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 41054731    245 DlTNTFRAIEFARDYAysqtSGGRPGATKVMVVV 278
Cdd:pfam13519   75 G-TNLAAALQLARAAL----KHRRKNQPRRIVLI 103
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 484-532 5.43e-07

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: 47.76  E-value: 5.43e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 41054731     484 IGSYFGSVLCSV-DVDKDTITDvLLVGAPTYMNDlkKEEGKVYLFTITKG 532
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRANDA--GETGAVYVYFGSSG 47
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 551-586 1.13e-06

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: 45.96  E-value: 1.13e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 41054731    551 FGSAIAALsDINMDGFNDVIVGSPVENE-NSGAVYIY 586
Cdd:pfam01839    1 FGYSVAVG-DLNGDGYADLAVGAPGEGGaGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 611-637 4.03e-04

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: 39.67  E-value: 4.03e-04
                            10        20
                    ....*....|....*....|....*..
gi 41054731     611 HLQFFGRSLDGYGDLNGDSITDVSIGA 637
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGA 27
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 44-92 4.81e-04

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: 39.28  E-value: 4.81e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 41054731      44 QFGYSVQQLTNPQGN---WLLVGSPWSGfPENRMGDVYKCPVDLPTATCEKL 92
Cdd:smart00191    4 YFGYSVAGVGDVNGDgypDLLVGAPRAN-DAGETGAVYVYFGSSGGGNSIPL 54
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 430-473 9.78e-04

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: 38.51  E-value: 9.78e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 41054731     430 HSSFLGYSVAAISTEDG---VHFVAGAPRAN---YTGQIVLYSVNKQGNV 473
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGdgyPDLLVGAPRANdagETGAVYVYFGSSGGGN 50
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 488-527 1.64e-03

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: 37.10  E-value: 1.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 41054731    488 FGSVLCSVDVDKDTITDvLLVGAPTYMNDlkkEEGKVYLF 527
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAPGEGGA---GAGAVYVL 36
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1152-1166 1.68e-03

Integrin alpha cytoplasmic region; This family contains the short intracellular region of integrin alpha chains.


Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.71  E-value: 1.68e-03
                           10
                   ....*....|....*
gi 41054731   1152 KLGFFKRQYKKMGQN 1166
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 560-633 1.82e-03

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: 37.59  E-value: 1.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41054731    560 DINMDGFNDVIVGspveNENSGAVYIYNGhQGTIrTKYSQKILGSNGAfrrhlqffGRSLDgYGDLNGDSITDV 633
Cdd:pfam13517    1 DLDGDGKLDLVVA----NDGGLRLYLNNG-DGTF-TFITSVSLGGGGG--------GLSVA-VGDLDGDGRLDL 59
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 171-288 4.38e-03

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


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 39.61  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054731  171 DVVVVCDESNSI--YPWEA-VKNFLVKFVTGLDIGPKKTQVALIQYANEPR--IIFNLNDFETKEDMVQATSETRQH--- 242
Cdd:cd01473    2 DLTLILDESASIgySNWRKdVIPFTEKIINNLNISKDKVHVGILLFAEKNRdvVPFSDEERYDKNELLKKINDLKNSyrs 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 41054731  243 GGDlTNTFRAIEFARdYAYSQTSGGRPGATKVMVVVTDGESHDGSK 288
Cdd:cd01473   82 GGE-TYIVEALKYGL-KNYTKHGNRRKDAPKVTMLFTDGNDTSASK 125
 
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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