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Conserved domains on  [gi|1358101459|ref|NP_001348174|]
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integrin alpha-E isoform 3 precursor [Mus musculus]

Protein Classification

vWA_integrins_alpha_subunit and Int_alpha domain-containing protein( domain architecture ID 11546366)

protein containing domains vWA_integrins_alpha_subunit, Int_alpha, and Integrin_alpha2

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 ...
 195-370 1.25e-87

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: 280.40  E-value: 1.25e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQVKEVTKTA 274
Cdd:cd01469      3 IVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNTA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  275 SAMQHVLDNIFIPSRGSRKKALKVMVVLTDGDIFGDPLnLTTVINSPKMQGVVRFAIGVGDAFKNNNTYRELKLIASDPK 354
Cdd:cd01469     83 TAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPL-LKDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASKPP 161

                          170
                   ....*....|....*.
gi 1358101459  355 EAHTFKVTNYSALDGL 370
Cdd:cd01469    162 EEHFFNVTDFAALKDI 177
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 668-938 6.67e-20

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: 94.31  E-value: 6.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  668 RPVVDLTVSMTFTPD---------ALPMVFIGKMDVKLCFEVDSSGVASePGLRemfLNFTVDVDVTKQR---QRLQCED 735
Cdd:pfam08441    1 RPVVSVSASLQVEPNsinpekkncTLTGTPVSCFTVRACFSYTGKPIPN-PSLV---LNYELELDRQKKKglpPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  736 SSGCQSCLRKW--NGGSFLCEHFWLISTEELceEDCFSNITIKVTYEFQTSG-GRRDYP--NPTLDHYKEPSAIFQLPYE 810
Cdd:pfam08441   77 SQQPSLTGTLVllSQGRKVCRTTKAYLRDEF--RDKLSPIVISLNYSLRVDPrAPSDLPglKPILDQNQPSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  811 KDCKNKVFCIAEIQLT----TNISQQELVVGVTKEVTMNISLTNSGEDSYMTNMALNYPRNLQFKKIQKPVS-PDVQCDD 885
Cdd:pfam08441  155 KDCGEDNVCVPDLQLSakfdSRESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSeKQLSCTA 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101459  886 PKPVASVLVMnCKIGHPILKRSSVNVSV---TWQLEESvfpNRTADITVTISNSNE 938
Cdd:pfam08441  235 KKENSTRQVV-CDLGNPMKRGTQVTFGLrfsVSGLELS---TEELSFDLQIRSTNE 286
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 565-624 2.48e-15

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: 71.25  E-value: 2.48e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459   565 NSRFGFAMAAVGDINQDKFTDVAIGAPlegfGAGDGASYGSVYIYNGHSGGLYDSPSQQI 624
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAP----RANDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 501-557 2.34e-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: 54.30  E-value: 2.34e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101459   501 MGSYFGSVLCPV-DIDMDGTTDfLLVAAPFYHIRGEEGRVYVYQVPEQDASFSLAHTL 557
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRANDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 635-658 5.58e-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: 38.90  E-value: 5.58e-04
                            10        20
                    ....*....|....*....|....
gi 1358101459   635 YFGMSVSGGLDFNGDGLADITVGS 658
Cdd:smart00191    4 YFGYSVAGVGDVNGDGYPDLLVGA 27
 
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 ...
 195-370 1.25e-87

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: 280.40  E-value: 1.25e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQVKEVTKTA 274
Cdd:cd01469      3 IVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNTA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  275 SAMQHVLDNIFIPSRGSRKKALKVMVVLTDGDIFGDPLnLTTVINSPKMQGVVRFAIGVGDAFKNNNTYRELKLIASDPK 354
Cdd:cd01469     83 TAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPL-LKDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASKPP 161

                          170
                   ....*....|....*.
gi 1358101459  355 EAHTFKVTNYSALDGL 370
Cdd:cd01469    162 EEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
195-373 1.69e-42

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 153.20  E-value: 1.69e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQV-KEVTKT 273
Cdd:pfam00092    2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  274 ASAMQHVLDNIFIPSRGSRKKALKVMVVLTDGDI-FGDPLnltTVINSPKMQGVVRFAIGVGDAfknnnTYRELKLIASD 352
Cdd:pfam00092   82 GKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDPE---EVARELKSAGVTVFAVGVGNA-----DDEELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 1358101459  353 PKEAHTFKVTNYSALDGLLSK 373
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 195-371 5.99e-36

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: 134.50  E-value: 5.99e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459   195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQV-KEVTKT 273
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTNL 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459   274 ASAMQHVLDNIFIPSRGSRKKALKVMVVLTDGDIFGDPLNLTTVINSPKMQGVVRFAIGVGdafkNNNTYRELKLIASDP 353
Cdd:smart00327   82 GAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVG----NDVDEEELKKLASAP 157

                           170
                    ....*....|....*...
gi 1358101459   354 KEAHTFKVTNYSALDGLL 371
Cdd:smart00327  158 GGVYVFLPELLDLLIDLL 175
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 668-938 6.67e-20

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: 94.31  E-value: 6.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  668 RPVVDLTVSMTFTPD---------ALPMVFIGKMDVKLCFEVDSSGVASePGLRemfLNFTVDVDVTKQR---QRLQCED 735
Cdd:pfam08441    1 RPVVSVSASLQVEPNsinpekkncTLTGTPVSCFTVRACFSYTGKPIPN-PSLV---LNYELELDRQKKKglpPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  736 SSGCQSCLRKW--NGGSFLCEHFWLISTEELceEDCFSNITIKVTYEFQTSG-GRRDYP--NPTLDHYKEPSAIFQLPYE 810
Cdd:pfam08441   77 SQQPSLTGTLVllSQGRKVCRTTKAYLRDEF--RDKLSPIVISLNYSLRVDPrAPSDLPglKPILDQNQPSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  811 KDCKNKVFCIAEIQLT----TNISQQELVVGVTKEVTMNISLTNSGEDSYMTNMALNYPRNLQFKKIQKPVS-PDVQCDD 885
Cdd:pfam08441  155 KDCGEDNVCVPDLQLSakfdSRESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSeKQLSCTA 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101459  886 PKPVASVLVMnCKIGHPILKRSSVNVSV---TWQLEESvfpNRTADITVTISNSNE 938
Cdd:pfam08441  235 KKENSTRQVV-CDLGNPMKRGTQVTFGLrfsVSGLELS---TEELSFDLQIRSTNE 286
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 565-624 2.48e-15

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: 71.25  E-value: 2.48e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459   565 NSRFGFAMAAVGDINQDKFTDVAIGAPlegfGAGDGASYGSVYIYNGHSGGLYDSPSQQI 624
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAP----RANDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 501-557 2.34e-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: 54.30  E-value: 2.34e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101459   501 MGSYFGSVLCPV-DIDMDGTTDfLLVAAPFYHIRGEEGRVYVYQVPEQDASFSLAHTL 557
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRANDAGETGAVYVYFGSSGGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 568-609 1.89e-05

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: 42.50  E-value: 1.89e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1358101459  568 FGFAmAAVGDINQDKFTDVAIGAPLEgfgagDGASYGSVYIY 609
Cdd:pfam01839    1 FGYS-VAVGDLNGDGYADLAVGAPGE-----GGAGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 505-542 3.47e-05

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: 41.73  E-value: 3.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1358101459  505 FGSVLCPVDIDMDGTTDfLLVAAPFYHIRGeEGRVYVY 542
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAPGEGGAG-AGAVYVL 36
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 195-346 3.19e-04

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: 43.77  E-value: 3.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGS-IEPSDFQKAKNFISTMMRNFYEKCfecNFALVQYGAVIQTEFDLqeSRDINASLAKVQSIvQVKEVTKT 273
Cdd:COG1240     95 VVLVVDASGSmAAENRLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLLPL--TRDREALKRALDEL-PPGGGTPL 168

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101459  274 ASAMQHVLDNIfipsRGSRKKALKVMVVLTDGDIFGDPLNLTTVINSPKMQGVVRFAIGVGDAFKNNNTYREL 346
Cdd:COG1240    169 GDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEGLLREI 237
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 635-658 5.58e-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: 38.90  E-value: 5.58e-04
                            10        20
                    ....*....|....*....|....
gi 1358101459   635 YFGMSVSGGLDFNGDGLADITVGS 658
Cdd:smart00191    4 YFGYSVAGVGDVNGDGYPDLLVGA 27
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 636-658 2.65e-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: 36.33  E-value: 2.65e-03
                           10        20
                   ....*....|....*....|...
gi 1358101459  636 FGMSVSGGlDFNGDGLADITVGS 658
Cdd:pfam01839    1 FGYSVAVG-DLNGDGYADLAVGA 22
 
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 ...
 195-370 1.25e-87

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: 280.40  E-value: 1.25e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQVKEVTKTA 274
Cdd:cd01469      3 IVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTNTA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  275 SAMQHVLDNIFIPSRGSRKKALKVMVVLTDGDIFGDPLnLTTVINSPKMQGVVRFAIGVGDAFKNNNTYRELKLIASDPK 354
Cdd:cd01469     83 TAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPL-LKDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASKPP 161

                          170
                   ....*....|....*.
gi 1358101459  355 EAHTFKVTNYSALDGL 370
Cdd:cd01469    162 EEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
195-373 1.69e-42

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 153.20  E-value: 1.69e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQV-KEVTKT 273
Cdd:pfam00092    2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  274 ASAMQHVLDNIFIPSRGSRKKALKVMVVLTDGDI-FGDPLnltTVINSPKMQGVVRFAIGVGDAfknnnTYRELKLIASD 352
Cdd:pfam00092   82 GKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDPE---EVARELKSAGVTVFAVGVGNA-----DDEELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 1358101459  353 PKEAHTFKVTNYSALDGLLSK 373
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 195-371 5.99e-36

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: 134.50  E-value: 5.99e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459   195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQV-KEVTKT 273
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTNL 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459   274 ASAMQHVLDNIFIPSRGSRKKALKVMVVLTDGDIFGDPLNLTTVINSPKMQGVVRFAIGVGdafkNNNTYRELKLIASDP 353
Cdd:smart00327   82 GAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVG----NDVDEEELKKLASAP 157

                           170
                    ....*....|....*...
gi 1358101459   354 KEAHTFKVTNYSALDGLL 371
Cdd:smart00327  158 GGVYVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 195-359 9.82e-27

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: 107.38  E-value: 9.82e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNF--YEKCFecNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQ-VKEVT 271
Cdd:cd01450      3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLdiGPDKT--RVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYlGGGGT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  272 KTASAMQHVLDNIFIPSRgSRKKALKVMVVLTDG--DIFGDPLNLTTVInspKMQGVVRFAIGVGDAFKNnntyrELKLI 349
Cdd:cd01450     81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGrsDDGGDPKEAAAKL---KDEGIKVFVVGVGPADEE-----ELREI 151

                          170
                   ....*....|
gi 1358101459  350 ASDPKEAHTF 359
Cdd:cd01450    152 ASCPSERHVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 195-364 1.29e-26

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: 107.37  E-value: 1.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQVKEVTKTA 274
Cdd:cd01482      3 IVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRTG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  275 SAMQHVLDNIFIPSRGSRKKALKVMVVLTDG---DifgdplNLTTVINSPKMQGVVRFAIGVGDAfknnnTYRELKLIAS 351
Cdd:cd01482     83 KALTHVREKNFTPDAGARPGVPKVVILITDGksqD------DVELPARVLRNLGVNVFAVGVKDA-----DESELKMIAS 151

                          170
                   ....*....|...
gi 1358101459  352 DPKEAHTFKVTNY 364
Cdd:cd01482    152 KPSETHVFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 195-363 2.17e-24

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: 100.77  E-value: 2.17e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQVKEVTKTA 274
Cdd:cd01472      3 IVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNTG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  275 SAMQHVLDNIFIPSRGSRKKALKVMVVLTDG----DIFGDPLNLTTVinspkmqGVVRFAIGVGDAFKNnntyrELKLIA 350
Cdd:cd01472     83 KALKYVRENLFTEASGSREGVPKVLVVITDGksqdDVEEPAVELKQA-------GIEVFAVGVKNADEE-----ELKQIA 150

                          170
                   ....*....|...
gi 1358101459  351 SDPKEAHTFKVTN 363
Cdd:cd01472    151 SDPKELYVFNVAD 163
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 198-378 6.02e-23

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: 98.61  E-value: 6.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  198 VLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIVQVKEVTKTASAM 277
Cdd:cd01475      8 LIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTMTGLAI 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  278 QHVLDNIFIPSRGSRKKAL---KVMVVLTDG---DIFGDplnlttVINSPKMQGVVRFAIGVGDAFKNnntyrELKLIAS 351
Cdd:cd01475     88 QYAMNNAFSEAEGARPGSErvpRVGIVVTDGrpqDDVSE------VAAKARALGIEMFAVGVGRADEE-----ELREIAS 156

                          170       180
                   ....*....|....*....|....*..
gi 1358101459  352 DPKEAHTFKVTNYSALDGLLSKLQQHI 378
Cdd:cd01475    157 EPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 195-359 6.14e-20

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 88.01  E-value: 6.14e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIV-QVKEVTKT 273
Cdd:cd00198      3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGTNI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  274 ASAMQHVLDNIFIPSRGSRKkalKVMVVLTDGDIFGDPLNLTTVINSPKMQGVVRFAIGVGDAFKNnntyRELKLIASDP 353
Cdd:cd00198     83 GAALRLALELLKSAKRPNAR---RVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANE----DELKEIADKT 155


                   ....*.
gi 1358101459  354 KEAHTF 359
Cdd:cd00198    156 TGGAVF 161
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 668-938 6.67e-20

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: 94.31  E-value: 6.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  668 RPVVDLTVSMTFTPD---------ALPMVFIGKMDVKLCFEVDSSGVASePGLRemfLNFTVDVDVTKQR---QRLQCED 735
Cdd:pfam08441    1 RPVVSVSASLQVEPNsinpekkncTLTGTPVSCFTVRACFSYTGKPIPN-PSLV---LNYELELDRQKKKglpPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  736 SSGCQSCLRKW--NGGSFLCEHFWLISTEELceEDCFSNITIKVTYEFQTSG-GRRDYP--NPTLDHYKEPSAIFQLPYE 810
Cdd:pfam08441   77 SQQPSLTGTLVllSQGRKVCRTTKAYLRDEF--RDKLSPIVISLNYSLRVDPrAPSDLPglKPILDQNQPSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  811 KDCKNKVFCIAEIQLT----TNISQQELVVGVTKEVTMNISLTNSGEDSYMTNMALNYPRNLQFKKIQKPVS-PDVQCDD 885
Cdd:pfam08441  155 KDCGEDNVCVPDLQLSakfdSRESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSeKQLSCTA 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1358101459  886 PKPVASVLVMnCKIGHPILKRSSVNVSV---TWQLEESvfpNRTADITVTISNSNE 938
Cdd:pfam08441  235 KKENSTRQVV-CDLGNPMKRGTQVTFGLrfsVSGLELS---TEELSFDLQIRSTNE 286
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 565-624 2.48e-15

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: 71.25  E-value: 2.48e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459   565 NSRFGFAMAAVGDINQDKFTDVAIGAPlegfGAGDGASYGSVYIYNGHSGGLYDSPSQQI 624
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAP----RANDAGETGAVYVYFGSSGGGNSIPLQNL 57
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 195-367 1.37e-10

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: 61.92  E-value: 1.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGA-----VIQTEFDLQESRDINASLAKVQ-SIVQVK 268
Cdd:cd01470      3 IYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASdpkeiVSIRDFNSNDADDVIKRLEDFNyDDHGDK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  269 EVTKTASAMQHVLDNIFIPSRGSRKKALK---VMVVLTDG--DIFGDPLNLTTVI-NSPKMQGVVR---------FAIGV 333
Cdd:cd01470     83 TGTNTAAALKKVYERMALEKVRNKEAFNEtrhVIILFTDGksNMGGSPLPTVDKIkNLVYKNNKSDnpredyldvYVFGV 162

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1358101459  334 GDAFKNNntyrELKLIASD-PKEAHTFKVTNYSAL 367
Cdd:cd01470    163 GDDVNKE----ELNDLASKkDNERHFFKLKDYEDL 193
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 195-359 1.98e-10

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: 60.49  E-value: 1.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSdFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQT--EFDLQESRDINASLAKVQSIVQVKEVTK 272
Cdd:cd01476      3 LLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTTA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  273 TASAMQHVLdNIFIPSRGSRKKALKVMVVLTDGDIFGDPLNLTTVINSPKmqGVVRFAIGVGDAFKNNNtyRELKLIASD 352
Cdd:cd01476     82 TGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVP--NIETFAVGTGDPGTVDT--EELHSITGN 156


                   ....*..
gi 1358101459  353 PKeaHTF 359
Cdd:cd01476    157 ED--HIF 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 195-368 2.12e-10

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: 61.25  E-value: 2.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNF---YEKCFE---CNFALVQY-GAVIQTEFDLQESRDInASLAK-VQSIVQ 266
Cdd:cd01480      5 ITFVLDSSESVGLQNFDITKNFVKRVAERFlkdYYRKDPagsWRVGVVQYsDQQEVEAGFLRDIRNY-TSLKEaVDNLEY 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  267 VKEVTKTASAMQHVLDNIFIpsrGSRKKALKVMVVLTDGDIFGDPLN-LTTVINSPKMQGVVRFAIGVGDAFKNNntyre 345
Cdd:cd01480     84 IGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDGSPDGgIEKAVNEADHLGIKIFFVAVGSQNEEP----- 155

                          170       180
                   ....*....|....*....|...
gi 1358101459  346 LKLIASDPKEAHtfKVTNYSALD 368
Cdd:cd01480    156 LSRIACDGKSAL--YRENFAELL 176
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 501-557 2.34e-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: 54.30  E-value: 2.34e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101459   501 MGSYFGSVLCPV-DIDMDGTTDfLLVAAPFYHIRGEEGRVYVYQVPEQDASFSLAHTL 557
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRANDAGETGAVYVYFGSSGGGNSIPLQNL 57
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 195-340 8.13e-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: 8.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSD-FQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAK-----VQSIVQVK 268
Cdd:cd01471      3 LYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALnairaLLSLYYPN 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1358101459  269 EVTKTASAMQHVLDNIFiPSRGSRKKALKVMVVLTDGdIFGDPLNLTTVINSPKMQGVVRFAIGVGDAFKNN 340
Cdd:cd01471     83 GSTNTTSALLVVEKHLF-DTRGNRENAPQLVIIMTDG-IPDSKFRTLKEARKLRERGVIIAVLGVGQGVNHE 152
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 195-353 3.64e-08

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: 54.25  E-value: 3.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEKCFECNFALVQYGAVIQTEFDLQESRDINASLAKVQSI-VQVKEVTKT 273
Cdd:cd01481      3 IVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLrLRGGSQLNT 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  274 ASAMQHVLDNIFIPSRGSR--KKALKVMVVLTDGDIFGDPLNLTTVInspKMQGVVRFAIGVGDAFKNnntyrELKLIAS 351
Cdd:cd01481     83 GSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVAL---KRAGIVPFAIGARNADLA-----ELQQIAF 154


                   ..
gi 1358101459  352 DP 353
Cdd:cd01481    155 DP 156
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 195-374 7.67e-08

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: 53.67  E-value: 7.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSI-----EPSDFQK--AKNFISTMMRnfyekcfecnFALVQYGAVIQTEFDLQESRD-INASLAKVQSIVQ 266
Cdd:cd01474      7 LYFVLDKSGSVaanwiEIYDFVEqlVDRFNSPGLR----------FSFITFSTRATKILPLTDDSSaIIKGLEVLKKVTP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  267 VKEvtktaSAMQHVLDN----IFIPSRGSRKKAlKVMVVLTDGDIFGDP-LNLTTVINSPKMQGVVRFAIGVGDAFKNnn 341
Cdd:cd01474     77 SGQ-----TYIHEGLENaneqIFNRNGGGRETV-SVIIALTDGQLLLNGhKYPEHEAKLSRKLGAIVYCVGVTDFLKS-- 148

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1358101459  342 tyrELKLIASDPKeaHTFKVTN-YSALDGLLSKL 374
Cdd:cd01474    149 ---QLINIADSKE--YVFPVTSgFQALSGIIESV 177
VWA_2 pfam13519
von Willebrand factor type A domain;
195-302 1.27e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 48.06  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSI-----EPSDFQKAKNFISTMMRNFYekcfECNFALVQYGAVIQTEFDLqeSRDINASLAKVQSIVQVKE 269
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPL--TKDRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1358101459  270 VTKTASAMQHVLDNIFipsrGSRKKALKVMVVL 302
Cdd:pfam13519   75 GTNLAAALQLARAALK----HRRKNQPRRIVLI 103
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 568-609 1.89e-05

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: 42.50  E-value: 1.89e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1358101459  568 FGFAmAAVGDINQDKFTDVAIGAPLEgfgagDGASYGSVYIY 609
Cdd:pfam01839    1 FGYS-VAVGDLNGDGYADLAVGAPGE-----GGAGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 505-542 3.47e-05

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: 41.73  E-value: 3.47e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1358101459  505 FGSVLCPVDIDMDGTTDfLLVAAPFYHIRGeEGRVYVY 542
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAPGEGGAG-AGAVYVL 36
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 577-654 1.46e-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: 40.67  E-value: 1.46e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1358101459  577 DINQDKFTDVAIgaplegfgagdgASYGSVYIYnghsggLYDSPSQQIRASSVASGLHYFGMSVSGGlDFNGDGLADI 654
Cdd:pfam13517    1 DLDGDGKLDLVV------------ANDGGLRLY------LNNGDGTFTFITSVSLGGGGGGLSVAVG-DLDGDGRLDL 59
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 195-346 3.19e-04

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: 43.77  E-value: 3.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGS-IEPSDFQKAKNFISTMMRNFYEKCfecNFALVQYGAVIQTEFDLqeSRDINASLAKVQSIvQVKEVTKT 273
Cdd:COG1240     95 VVLVVDASGSmAAENRLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLLPL--TRDREALKRALDEL-PPGGGTPL 168

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1358101459  274 ASAMQHVLDNIfipsRGSRKKALKVMVVLTDGDIFGDPLNLTTVINSPKMQGVVRFAIGVGDAFKNNNTYREL 346
Cdd:COG1240    169 GDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEGLLREI 237
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 635-658 5.58e-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: 38.90  E-value: 5.58e-04
                            10        20
                    ....*....|....*....|....
gi 1358101459   635 YFGMSVSGGLDFNGDGLADITVGS 658
Cdd:smart00191    4 YFGYSVAGVGDVNGDGYPDLLVGA 27
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 636-658 2.65e-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: 36.33  E-value: 2.65e-03
                           10        20
                   ....*....|....*....|...
gi 1358101459  636 FGMSVSGGlDFNGDGLADITVGS 658
Cdd:pfam01839    1 FGYSVAVG-DLNGDGYADLAVGA 22
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 195-338 9.24e-03

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 39.31  E-value: 9.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1358101459  195 IAIVLDGSGSIEPSDFQKAKNFISTMMRNFYEkcfECNFALVQYGAVIQTEFDLQESRDINASLAKVQSIvQVKEVTKTA 274
Cdd:COG2304     94 LVFVIDVSGSMSGDKLELAKEAAKLLVDQLRP---GDRVSIVTFAGDARVLLPPTPATDRAKILAAIDRL-QAGGGTALG 169

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1358101459  275 SAMQHVLDnifIPSRGSRKKALKVMVVLTDGDI---FGDPLNLTTVINSPKMQGVVRFAIGVGDAFK 338
Cdd:COG2304    170 AGLELAYE---LARKHFIPGRVNRVILLTDGDAnvgITDPEELLKLAEEAREEGITLTTLGVGSDYN 233
 
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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