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Conserved domains on  [gi|148728188|ref|NP_002199|]
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integrin alpha-E isoform 1 precursor [Homo sapiens]

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 ...
 201-378 4.09e-74

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: 243.03  E-value: 4.09e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  201 TEIAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNITQVGSVTK 280
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  281 TASAMQHVLDSIFTSSHGSRRKASKVMVVLTDGGIFEDPLnLTTVINSPKMQGVERFAIGVGEEFKSARTARELNLIASD 360
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPL-LKDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 148728188  361 PDETHAFKVTNYMALDGL 378
Cdd:cd01469   160 PPEEHFFNVTDFAALKDI 177
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 677-951 4.96e-17

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: 85.45  E-value: 4.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   677 RPVVRLKVSMAFTPSAL-------PIGFNGV--VNVRLCFEISSVTTASESgLRealLNFTLDVDVGKQRRRL------- 740
Cdd:pfam08441    1 RPVVSVSASLQVEPNSInpekkncTLTGTPVscFTVRACFSYTGKPIPNPS-LV---LNYELELDRQKKKGLPprvlfld 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   741 -QCSDVRscLGCLREwSSGSQLCEDLLLMptegeLCEE--DCFS--NASVKVSYQLQTPEGQTDHP-QPILDRYTEPFAI 814
Cdd:pfam08441   77 sQQPSLT--GTLVLL-SQGRKVCRTTKAY-----LRDEfrDKLSpiVISLNYSLRVDPRAPSDLPGlKPILDQNQPSTVQ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   815 FQLPYEKACKNKLFCVAELQLA----TTVSQQELVVGLTKELTLNINLTNSGEDSYMTSMALNYPRNLQLKRMQKP-PSP 889
Cdd:pfam08441  149 EQANFLKDCGEDNVCVPDLQLSakfdSRESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREgSEK 228

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148728188   890 NIQCDDPQpVASVLIMNCRIGHPVLKRSSAHVSVVWQLEENAFPNRTADITVTVTNSNERRS 951
Cdd:pfam08441  229 QLSCTAKK-ENSTRQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS 289
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 574-633 5.89e-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: 64.32  E-value: 5.89e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188    574 NARFGFAMAAMGDLSQDKLTDVAIGAPlegfGADDGASFGSVYIYNGHWDGLSASPSQRI 633
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAP----RANDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 510-561 1.99e-10

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: 57.39  E-value: 1.99e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 148728188    510 MGSYFGSELCPV-DIDMDGSTDfLLVAAPFYHVHGEEGRVYVYRLSEQDGSFS 561
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRANDAGETGAVYVYFGSSGGGNSI 52
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 643-678 8.12e-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: 8.12e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 148728188    643 QYFGMSMAGGFDISGDGLADITVG--------TLGQAVVFRSRP 678
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGaprandagETGAVYVYFGSS 46
 
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 ...
 201-378 4.09e-74

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: 243.03  E-value: 4.09e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  201 TEIAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNITQVGSVTK 280
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  281 TASAMQHVLDSIFTSSHGSRRKASKVMVVLTDGGIFEDPLnLTTVINSPKMQGVERFAIGVGEEFKSARTARELNLIASD 360
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPL-LKDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 148728188  361 PDETHAFKVTNYMALDGL 378
Cdd:cd01469   160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
202-381 3.97e-45

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 160.52  E-value: 3.97e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   202 EIAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNITQV-GSVTK 280
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   281 TASAMQHVLDSIFTSSHGSRRKASKVMVVLTDgGIFEDPlNLTTVINSPKMQGVERFAIGVGEefksaRTARELNLIASD 360
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTD-GRSQDG-DPEEVARELKSAGVTVFAVGVGN-----ADDEELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 148728188   361 PDETHAFKVTNYMALDGLLSK 381
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 203-379 3.17e-35

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: 132.19  E-value: 3.17e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188    203 IAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNITQV-GSVTKT 281
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTNL 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188    282 ASAMQHVLDSIFTSSHGSRRKASKVMVVLTDGGIFEDPLNLTTVINSPKMQGVERFAIGVGEEFKSArtarELNLIASDP 361
Cdd:smart00327   82 GAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEE----ELKKLASAP 157

                           170
                    ....*....|....*...
gi 148728188    362 DETHAFKVTNYMALDGLL 379
Cdd:smart00327  158 GGVYVFLPELLDLLIDLL 175
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 677-951 4.96e-17

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: 85.45  E-value: 4.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   677 RPVVRLKVSMAFTPSAL-------PIGFNGV--VNVRLCFEISSVTTASESgLRealLNFTLDVDVGKQRRRL------- 740
Cdd:pfam08441    1 RPVVSVSASLQVEPNSInpekkncTLTGTPVscFTVRACFSYTGKPIPNPS-LV---LNYELELDRQKKKGLPprvlfld 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   741 -QCSDVRscLGCLREwSSGSQLCEDLLLMptegeLCEE--DCFS--NASVKVSYQLQTPEGQTDHP-QPILDRYTEPFAI 814
Cdd:pfam08441   77 sQQPSLT--GTLVLL-SQGRKVCRTTKAY-----LRDEfrDKLSpiVISLNYSLRVDPRAPSDLPGlKPILDQNQPSTVQ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   815 FQLPYEKACKNKLFCVAELQLA----TTVSQQELVVGLTKELTLNINLTNSGEDSYMTSMALNYPRNLQLKRMQKP-PSP 889
Cdd:pfam08441  149 EQANFLKDCGEDNVCVPDLQLSakfdSRESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREgSEK 228

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148728188   890 NIQCDDPQpVASVLIMNCRIGHPVLKRSSAHVSVVWQLEENAFPNRTADITVTVTNSNERRS 951
Cdd:pfam08441  229 QLSCTAKK-ENSTRQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS 289
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 574-633 5.89e-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: 64.32  E-value: 5.89e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188    574 NARFGFAMAAMGDLSQDKLTDVAIGAPlegfGADDGASFGSVYIYNGHWDGLSASPSQRI 633
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAP----RANDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 510-561 1.99e-10

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: 57.39  E-value: 1.99e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 148728188    510 MGSYFGSELCPV-DIDMDGSTDfLLVAAPFYHVHGEEGRVYVYRLSEQDGSFS 561
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRANDAGETGAVYVYFGSSGGGNSI 52
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 200-354 7.23e-08

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: 54.94  E-value: 7.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  200 GTEIAIILDGSGSIDPPD-FQRAKDFISNMMRNFYEKCfecNFALVQYGGVIQTEFDL-RDSQDVMASLARVQnitqVGS 277
Cdd:COG1240    92 GRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLLPLtRDREALKRALDELP----PGG 164

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148728188  278 VTKTASAMQHVLDsIFTSSHGSRRKaskVMVVLTDGGIFEDPLNLTTVINSPKMQGVERFAIGVGEEFKSARTAREL 354
Cdd:COG1240   165 GTPLGDALALALE-LLKRADPARRK---VIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEGLLREI 237
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 514-551 3.61e-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: 3.61e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 148728188   514 FGSELCPVDIDMDGSTDfLLVAAPFYHVHGeEGRVYVY 551
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAPGEGGAG-AGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 643-678 8.12e-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: 8.12e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 148728188    643 QYFGMSMAGGFDISGDGLADITVG--------TLGQAVVFRSRP 678
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGaprandagETGAVYVYFGSS 46
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 577-618 1.14e-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: 37.49  E-value: 1.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 148728188   577 FGFAMAAmGDLSQDKLTDVAIGAPLEgfgadDGASFGSVYIY 618
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGE-----GGAGAGAVYVL 36
 
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 ...
 201-378 4.09e-74

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: 243.03  E-value: 4.09e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  201 TEIAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNITQVGSVTK 280
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  281 TASAMQHVLDSIFTSSHGSRRKASKVMVVLTDGGIFEDPLnLTTVINSPKMQGVERFAIGVGEEFKSARTARELNLIASD 360
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPL-LKDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 148728188  361 PDETHAFKVTNYMALDGL 378
Cdd:cd01469   160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
202-381 3.97e-45

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 160.52  E-value: 3.97e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   202 EIAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNITQV-GSVTK 280
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLgGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   281 TASAMQHVLDSIFTSSHGSRRKASKVMVVLTDgGIFEDPlNLTTVINSPKMQGVERFAIGVGEefksaRTARELNLIASD 360
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTD-GRSQDG-DPEEVARELKSAGVTVFAVGVGN-----ADDEELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 148728188   361 PDETHAFKVTNYMALDGLLSK 381
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 203-379 3.17e-35

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: 132.19  E-value: 3.17e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188    203 IAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNITQV-GSVTKT 281
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKlGGGTNL 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188    282 ASAMQHVLDSIFTSSHGSRRKASKVMVVLTDGGIFEDPLNLTTVINSPKMQGVERFAIGVGEEFKSArtarELNLIASDP 361
Cdd:smart00327   82 GAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEE----ELKKLASAP 157

                           170
                    ....*....|....*...
gi 148728188    362 DETHAFKVTNYMALDGLL 379
Cdd:smart00327  158 GGVYVFLPELLDLLIDLL 175
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 201-372 1.21e-29

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: 115.85  E-value: 1.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  201 TEIAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDL---RDSQDVMASlarVQNITQVGS 277
Cdd:cd01482     1 ADIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLnayTSKEDVLAA---IKNLPYKGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  278 VTKTASAMQHVLDSIFTSSHGSRRKASKVMVVLTDGGIFEDplnlttvINSP----KMQGVERFAIGVgeefKSArTARE 353
Cdd:cd01482    78 NTRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDD-------VELParvlRNLGVNVFAVGV----KDA-DESE 145

                         170
                  ....*....|....*....
gi 148728188  354 LNLIASDPDETHAFKVTNY 372
Cdd:cd01482   146 LKMIASKPSETHVFNVADF 164
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 203-367 1.16e-28

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


Pssm-ID: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 113.16  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  203 IAIILDGSGSIDPPDFQRAKDFISNMMRNF--YEKCFecNFALVQYGGVIQTEFDLRDSQ---DVMASLARVQNITqvGS 277
Cdd:cd01450     3 IVFLLDGSESVGPENFEKVKDFIEKLVEKLdiGPDKT--RVGLVQYSDDVRVEFSLNDYKskdDLLKAVKNLKYLG--GG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  278 VTKTASAMQHVLDSIFTSShGSRRKASKVMVVLTDgGIFEDPLNLTTVINSPKMQGVERFAIGVGEEFKSartarELNLI 357
Cdd:cd01450    79 GTNTGKALQYALEQLFSES-NARENVPKVIIVLTD-GRSDDGGDPKEAAAKLKDEGIKVFVVGVGPADEE-----ELREI 151

                         170
                  ....*....|
gi 148728188  358 ASDPDETHAF 367
Cdd:cd01450   152 ASCPSERHVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 203-371 7.89e-26

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: 105.00  E-value: 7.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  203 IAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDL---RDSQDVMASLARVQNItqvGSVT 279
Cdd:cd01472     3 IVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLntyRSKDDVLEAVKNLRYI---GGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  280 KTASAMQHVLDSIFTSSHGSRRKASKVMVVLTDGGIfEDPLNLTTVinSPKMQGVERFAIGVGEEFKSartarELNLIAS 359
Cdd:cd01472    80 NTGKALKYVRENLFTEASGSREGVPKVLVVITDGKS-QDDVEEPAV--ELKQAGIEVFAVGVKNADEE-----ELKQIAS 151

                         170
                  ....*....|..
gi 148728188  360 DPDETHAFKVTN 371
Cdd:cd01472   152 DPKELYVFNVAD 163
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 203-367 1.77e-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: 89.55  E-value: 1.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  203 IAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNIT-QVGSVTKT 281
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGTNI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  282 ASAMQHVLDSIFTSSHGSRRkasKVMVVLTDGGIFEDPLNLTTVINSPKMQGVERFAIGVGEEFKSArtarELNLIASDP 361
Cdd:cd00198    83 GAALRLALELLKSAKRPNAR---RVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANED----ELKEIADKT 155


                  ....*.
gi 148728188  362 DETHAF 367
Cdd:cd00198   156 TGGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 201-386 4.32e-19

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: 87.44  E-value: 4.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  201 TEIAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNITQVGSVTK 280
Cdd:cd01475     3 TDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  281 TASAMQHVLDSIFTSSHGSR---RKASKVMVVLTDGGIfEDPLNltTVINSPKMQGVERFAIGVGEEFKSartarELNLI 357
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGRP-QDDVS--EVAAKARALGIEMFAVGVGRADEE-----ELREI 154

                         170       180
                  ....*....|....*....|....*....
gi 148728188  358 ASDPDETHAFKVTNYMALDGLLSKLRYNI 386
Cdd:cd01475   155 ASEPLADHVFYVEDFSTIEELTKKFQGKI 183
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 677-951 4.96e-17

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: 85.45  E-value: 4.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   677 RPVVRLKVSMAFTPSAL-------PIGFNGV--VNVRLCFEISSVTTASESgLRealLNFTLDVDVGKQRRRL------- 740
Cdd:pfam08441    1 RPVVSVSASLQVEPNSInpekkncTLTGTPVscFTVRACFSYTGKPIPNPS-LV---LNYELELDRQKKKGLPprvlfld 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   741 -QCSDVRscLGCLREwSSGSQLCEDLLLMptegeLCEE--DCFS--NASVKVSYQLQTPEGQTDHP-QPILDRYTEPFAI 814
Cdd:pfam08441   77 sQQPSLT--GTLVLL-SQGRKVCRTTKAY-----LRDEfrDKLSpiVISLNYSLRVDPRAPSDLPGlKPILDQNQPSTVQ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   815 FQLPYEKACKNKLFCVAELQLA----TTVSQQELVVGLTKELTLNINLTNSGEDSYMTSMALNYPRNLQLKRMQKP-PSP 889
Cdd:pfam08441  149 EQANFLKDCGEDNVCVPDLQLSakfdSRESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREgSEK 228

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148728188   890 NIQCDDPQpVASVLIMNCRIGHPVLKRSSAHVSVVWQLEENAFPNRTADITVTVTNSNERRS 951
Cdd:pfam08441  229 QLSCTAKK-ENSTRQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS 289
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 574-633 5.89e-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: 64.32  E-value: 5.89e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188    574 NARFGFAMAAMGDLSQDKLTDVAIGAPlegfGADDGASFGSVYIYNGHWDGLSASPSQRI 633
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAP----RANDAGETGAVYVYFGSSGGGNSIPLQNL 57
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 202-367 6.51e-13

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 67.81  E-value: 6.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  202 EIAIILDGSGSIDPpDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQT--EFDLRDSQDVMASLARVQNITQVGSVT 279
Cdd:cd01476     2 DLLFVLDSSGSVRG-KFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  280 KTASAMQHVLDsIFTSSHGSRRKASKVMVVLTDGGIFEDPLNLTTVINSPKmqGVERFAIGVGEEFKSARtaRELNLIAS 359
Cdd:cd01476    81 ATGAAIEVALQ-QLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAVP--NIETFAVGTGDPGTVDT--EELHSITG 155


                  ....*...
gi 148728188  360 DPDetHAF 367
Cdd:cd01476   156 NED--HIF 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 202-362 1.10e-11

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: 64.27  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  202 EIAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLR---DSQDVMASLARVQniTQVGSV 278
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNthsTKADVLGAVRRLR--LRGGSQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  279 TKTASAMQHVLDSIFTSSHGSR-RKASKVMVVLTDGGIFEDPLNLTTviNSPKMQGVERFAIGVgeefKSARTArELNLI 357
Cdd:cd01481    80 LNTGSALDYVVKNLFTKSAGSRiEEGVPQFLVLITGGKSQDDVERPA--VALKRAGIVPFAIGA----RNADLA-ELQQI 152


                  ....*
gi 148728188  358 ASDPD 362
Cdd:cd01481   153 AFDPS 157
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 510-561 1.99e-10

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: 57.39  E-value: 1.99e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 148728188    510 MGSYFGSELCPV-DIDMDGSTDfLLVAAPFYHVHGEEGRVYVYRLSEQDGSFS 561
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPRANDAGETGAVYVYFGSSGGGNSI 52
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 203-365 1.54e-09

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: 58.55  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  203 IAIILDGSGSIDPPDFQRAKDFISNMMRNF---YEKCFE---CNFALVQY-GGVIQTEFDLRDSQDvMASLAR-VQNITQ 274
Cdd:cd01480     5 ITFVLDSSESVGLQNFDITKNFVKRVAERFlkdYYRKDPagsWRVGVVQYsDQQEVEAGFLRDIRN-YTSLKEaVDNLEY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  275 VGSVTKTASAMQHVLDSIFtssHGSRRKASKVMVVLTDGGIF-EDPLNLTTVINSPKMQGVERFAIGVGEEFKSartarE 353
Cdd:cd01480    84 IGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDgSPDGGIEKAVNEADHLGIKIFFVAVGSQNEE-----P 155

                         170
                  ....*....|..
gi 148728188  354 LNLIASDPDETH 365
Cdd:cd01480   156 LSRIACDGKSAL 167
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 203-375 2.73e-09

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: 58.07  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  203 IAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGG-----VIQTEFDLRDSQDVMASLARVQ-NITQVG 276
Cdd:cd01470     3 IYIALDASDSIGEEDFDEAKNAIKTLIEKISSYEVSPRYEIISYASdpkeiVSIRDFNSNDADDVIKRLEDFNyDDHGDK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  277 SVTKTASAMQHVLDSIFTSSHGSRRKASK---VMVVLTD-----GGifeDPLNLTTVI------NSPKMQGVER----FA 338
Cdd:cd01470    83 TGTNTAAALKKVYERMALEKVRNKEAFNEtrhVIILFTDgksnmGG---SPLPTVDKIknlvykNNKSDNPREDyldvYV 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 148728188  339 IGVGEEFKSartaRELNLIASD-PDETHAFKVTNYMAL 375
Cdd:cd01470   160 FGVGDDVNK----EELNDLASKkDNERHFFKLKDYEDL 193
VWA_2 pfam13519
von Willebrand factor type A domain;
203-310 1.85e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 53.06  E-value: 1.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188   203 IAIILDGSGSIDPPD-----FQRAKDFISNMMRNFYekcfECNFALVQYGGVIQTEFDLRDSQDVMasLARVQNITQVGS 277
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSLP----GDRVGLVTFGDGPEVLIPLTKDRAKI--LRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 148728188   278 VTKTASAMQHVLDSIFTsshgSRRKASKVMVVL 310
Cdd:pfam13519   75 GTNLAAALQLARAALKH----RRKNQPRRIVLI 103
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 200-354 7.23e-08

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: 54.94  E-value: 7.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  200 GTEIAIILDGSGSIDPPD-FQRAKDFISNMMRNFYEKCfecNFALVQYGGVIQTEFDL-RDSQDVMASLARVQnitqVGS 277
Cdd:COG1240    92 GRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPRD---RVGLVAFGGEAEVLLPLtRDREALKRALDELP----PGG 164

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148728188  278 VTKTASAMQHVLDsIFTSSHGSRRKaskVMVVLTDGGIFEDPLNLTTVINSPKMQGVERFAIGVGEEFKSARTAREL 354
Cdd:COG1240   165 GTPLGDALALALE-LLKRADPARRK---VIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEGLLREI 237
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 202-342 4.91e-06

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: 48.54  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  202 EIAIILDGSGSIDPPD-FQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLAR-----VQNITQV 275
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALnairaLLSLYYP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148728188  276 GSVTKTASAMQHVLDSIFTSShGSRRKASKVMVVLTDgGIFEDPLNLTTVINSPKMQGVERFAIGVG 342
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTD-GIPDSKFRTLKEARKLRERGVIIAVLGVG 146
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 514-551 3.61e-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: 3.61e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 148728188   514 FGSELCPVDIDMDGSTDfLLVAAPFYHVHGeEGRVYVY 551
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAPGEGGAG-AGAVYVL 36
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 200-382 5.97e-05

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: 45.19  E-value: 5.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  200 GTEIAIILDGSGSIDPP-----DF--QRAKDFISNMMRnfyekcfecnFALVQYGGVIQTEFDLR-DSQDVMASLARVQN 271
Cdd:cd01474     4 HFDLYFVLDKSGSVAANwieiyDFveQLVDRFNSPGLR----------FSFITFSTRATKILPLTdDSSAIIKGLEVLKK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148728188  272 ITQVGSvTKTASAMQHVLDSIFTSSHGSRRKASkVMVVLTDGGIFEDP-LNLTTVINSPKMQGVERFAIGVGEEFKSart 350
Cdd:cd01474    74 VTPSGQ-TYIHEGLENANEQIFNRNGGGRETVS-VIIALTDGQLLLNGhKYPEHEAKLSRKLGAIVYCVGVTDFLKS--- 148

                         170       180       190
                  ....*....|....*....|....*....|...
gi 148728188  351 arELNLIASDPDetHAFKVTN-YMALDGLLSKL 382
Cdd:cd01474   149 --QLINIADSKE--YVFPVTSgFQALSGIIESV 177
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 643-678 8.12e-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: 8.12e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 148728188    643 QYFGMSMAGGFDISGDGLADITVG--------TLGQAVVFRSRP 678
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGaprandagETGAVYVYFGSS 46
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 577-618 1.14e-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: 37.49  E-value: 1.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 148728188   577 FGFAMAAmGDLSQDKLTDVAIGAPLEgfgadDGASFGSVYIY 618
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGE-----GGAGAGAVYVL 36
 
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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