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Conserved domains on  [gi|568949728|ref|XP_006507456.1|]
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PREDICTED: integrin alpha-L isoform X1 [Mus musculus]

Protein Classification

vWFA and Int_alpha domain-containing protein (domain architecture ID 11619899)

protein containing domains vWFA, Int_alpha, and Integrin_alpha2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
152-321 1.24e-59

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


The actual alignment was detected with superfamily member cd01469:

Pssm-ID: 320736  Cd Length: 177  Bit Score: 201.43  E-value: 1.24e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 152 VDLVFLFDGSQSLDRKDFEKILEFMKDVMRKLSN--TSYQFAAVQFSTDCRTEFTFLDYVKqNKNPDVLLGSVQPMFLLT 229
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRT-KEEPLSLVKHISQLLGLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 230 NTFRAINYVVAHVFKEESGARPDATKVLVIITDGEASD----KGNISAAH--DITRYIIGIGKHFVSVQKQKTLHIFASE 303
Cdd:cd01469   80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASK 159
                        170
                 ....*....|....*...
gi 568949728 304 PVEEFVKILDTFEKLKDL 321
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
515-567 2.06e-11

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  Cd Length: 57  Bit Score: 61.62  E-value: 2.06e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949728   515 PLGRFGAAITALTDINGDRLTDVAVGAPLE----EQGAVYIFNGKPGGLSPQPSQRI 567
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
610-740 2.68e-10

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: 312071  Cd Length: 447  Bit Score: 63.10  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728  610 SRPVVDVVTELSFSPEEIPVHEVECsysarEEQKHG----VKLKACFRI--KPLTPQfqgRLlaNLSYTLQLD---GHRM 680
Cdd:pfam08441   1 ARPVVNVNASLTVEPNSINLDKKNC-----TLPTGTpvscFTVRACFSYtgKPVYPP---SL--DLNYELELDslkKKGR 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949728  681 RSRGLFPDG-SHELSGNTSITPDKS--CLDFHFHFPICIQDLISPINVSLNFSLLEEEGTPRD 740
Cdd:pfam08441  71 PPRVLFLDSqQPSLTTTLVLLSQGRkvCRDLTAYLRDNFRDKLTPIVIELNYSLRVPPRAKRA 133
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
454-500 5.71e-05

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


:

Pssm-ID: 214549  Cd Length: 57  Bit Score: 42.75  E-value: 5.71e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568949728   454 IGSYFGGELCSV-DLDQDGEAELLlIGAPLFFGEQRGGRVFTYQRRQS 500
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSG 47
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
399-449 8.77e-05

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


:

Pssm-ID: 214549  Cd Length: 57  Bit Score: 42.36  E-value: 8.77e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949728   399 GGYLGYTVAWMT--SRSSRPLLAAGAPRYQH---VGQVLLFQAPEAGGRWNQTQKI 449
Cdd:smart00191   2 GSYFGYSVAGVGdvNGDGYPDLLVGAPRANDageTGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
578-622 9.72e-03

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  Cd Length: 57  Bit Score: 36.20  E-value: 9.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568949728   578 WFGRSIHGVKDLGGDRLADVVVGA--------EGRVVVLSSRPVVDVVTELSF 622
Cdd:smart00191   4 YFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
 
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 ...
152-321 1.24e-59

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  Cd Length: 177  Bit Score: 201.43  E-value: 1.24e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 152 VDLVFLFDGSQSLDRKDFEKILEFMKDVMRKLSN--TSYQFAAVQFSTDCRTEFTFLDYVKqNKNPDVLLGSVQPMFLLT 229
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRT-KEEPLSLVKHISQLLGLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 230 NTFRAINYVVAHVFKEESGARPDATKVLVIITDGEASD----KGNISAAH--DITRYIIGIGKHFVSVQKQKTLHIFASE 303
Cdd:cd01469   80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASK 159
                        170
                 ....*....|....*...
gi 568949728 304 PVEEFVKILDTFEKLKDL 321
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
153-324 4.81e-41

von Willebrand factor type A domain;


Pssm-ID: 306576  Cd Length: 174  Bit Score: 149.35  E-value: 4.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728  153 DLVFLFDGSQSLDRKDFEKILEFMKDVMRKL--SNTSYQFAAVQFSTDCRTEFTFLDYvkqnKNPDVLLGSVQPMFLL-- 228
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLSKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDY----SSKEELLSAVDNLRYSgg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728  229 --TNTFRAINYVVAHVFKEESGARPDATKVLVIITDGEASDKGNISAAH-----DITRYIIGIGKHFVsvqkqKTLHIFA 301
Cdd:pfam00092  77 gtTNTGKALKYALENLFSSSAGARPGVPKVVVLLTDGRSQDGDPEEAARelksaGVTVFAVGVGNADN-----EELNKIA 151
                         170       180
                  ....*....|....*....|...
gi 568949728  302 SEPVEEFVKILDTFEKLKDLFTD 324
Cdd:pfam00092 152 SEPDEGHVFTVSDFEALQDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
153-318 1.72e-29

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  Cd Length: 175  Bit Score: 117.17  E-value: 1.72e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728   153 DLVFLFDGSQSLDRKDFEKILEFMKDVMRKL--SNTSYQFAAVQFSTDCRTEFTFLDYvkqnKNPDVLLGSVQPMFLL-- 228
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDS----RSKDALLEALASLSYKlg 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728   229 --TNTFRAINYVVAHVFKEESGARPDATKVLVIITDGEASDKGN-----ISAAHD--ITRYIIGIGKHFvsvqKQKTLHI 299
Cdd:smart00327  77 ggTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdllkaAKELKRsgVKVFVVGVGNDV----DEEELKK 152
                          170
                   ....*....|....*....
gi 568949728   300 FASEPVEEFVKILDTFEKL 318
Cdd:smart00327 153 LASAPGGVYVFLPELLDLL 171
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
515-567 2.06e-11

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  Cd Length: 57  Bit Score: 61.62  E-value: 2.06e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949728   515 PLGRFGAAITALTDINGDRLTDVAVGAPLE----EQGAVYIFNGKPGGLSPQPSQRI 567
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
610-740 2.68e-10

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: 312071  Cd Length: 447  Bit Score: 63.10  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728  610 SRPVVDVVTELSFSPEEIPVHEVECsysarEEQKHG----VKLKACFRI--KPLTPQfqgRLlaNLSYTLQLD---GHRM 680
Cdd:pfam08441   1 ARPVVNVNASLTVEPNSINLDKKNC-----TLPTGTpvscFTVRACFSYtgKPVYPP---SL--DLNYELELDslkKKGR 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949728  681 RSRGLFPDG-SHELSGNTSITPDKS--CLDFHFHFPICIQDLISPINVSLNFSLLEEEGTPRD 740
Cdd:pfam08441  71 PPRVLFLDSqQPSLTTTLVLLSQGRkvCRDLTAYLRDNFRDKLTPIVIELNYSLRVPPRAKRA 133
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
454-500 5.71e-05

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


Pssm-ID: 214549  Cd Length: 57  Bit Score: 42.75  E-value: 5.71e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568949728   454 IGSYFGGELCSV-DLDQDGEAELLlIGAPLFFGEQRGGRVFTYQRRQS 500
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSG 47
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
519-552 8.38e-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: 307792  Cd Length: 36  Bit Score: 42.14  E-value: 8.38e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568949728  519 FGAAItALTDINGDRLTDVAVGAPL---EEQGAVYIF 552
Cdd:pfam01839   1 FGSSV-AVGDLNGDGYADLAVGAPAaggTGGGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
399-449 8.77e-05

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


Pssm-ID: 214549  Cd Length: 57  Bit Score: 42.36  E-value: 8.77e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949728   399 GGYLGYTVAWMT--SRSSRPLLAAGAPRYQH---VGQVLLFQAPEAGGRWNQTQKI 449
Cdd:smart00191   2 GSYFGYSVAGVGdvNGDGYPDLLVGAPRANDageTGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
578-622 9.72e-03

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  Cd Length: 57  Bit Score: 36.20  E-value: 9.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568949728   578 WFGRSIHGVKDLGGDRLADVVVGA--------EGRVVVLSSRPVVDVVTELSF 622
Cdd:smart00191   4 YFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
 
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 ...
152-321 1.24e-59

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  Cd Length: 177  Bit Score: 201.43  E-value: 1.24e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 152 VDLVFLFDGSQSLDRKDFEKILEFMKDVMRKLSN--TSYQFAAVQFSTDCRTEFTFLDYVKqNKNPDVLLGSVQPMFLLT 229
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRT-KEEPLSLVKHISQLLGLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 230 NTFRAINYVVAHVFKEESGARPDATKVLVIITDGEASD----KGNISAAH--DITRYIIGIGKHFVSVQKQKTLHIFASE 303
Cdd:cd01469   80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASK 159
                        170
                 ....*....|....*...
gi 568949728 304 PVEEFVKILDTFEKLKDL 321
Cdd:cd01469  160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
153-324 4.81e-41

von Willebrand factor type A domain;


Pssm-ID: 306576  Cd Length: 174  Bit Score: 149.35  E-value: 4.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728  153 DLVFLFDGSQSLDRKDFEKILEFMKDVMRKL--SNTSYQFAAVQFSTDCRTEFTFLDYvkqnKNPDVLLGSVQPMFLL-- 228
Cdd:pfam00092   1 DIVFLLDGSGSIGGDNFEKVKEFLSKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDY----SSKEELLSAVDNLRYSgg 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728  229 --TNTFRAINYVVAHVFKEESGARPDATKVLVIITDGEASDKGNISAAH-----DITRYIIGIGKHFVsvqkqKTLHIFA 301
Cdd:pfam00092  77 gtTNTGKALKYALENLFSSSAGARPGVPKVVVLLTDGRSQDGDPEEAARelksaGVTVFAVGVGNADN-----EELNKIA 151
                         170       180
                  ....*....|....*....|...
gi 568949728  302 SEPVEEFVKILDTFEKLKDLFTD 324
Cdd:pfam00092 152 SEPDEGHVFTVSDFEALQDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
153-318 1.72e-29

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  Cd Length: 175  Bit Score: 117.17  E-value: 1.72e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728   153 DLVFLFDGSQSLDRKDFEKILEFMKDVMRKL--SNTSYQFAAVQFSTDCRTEFTFLDYvkqnKNPDVLLGSVQPMFLL-- 228
Cdd:smart00327   1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDS----RSKDALLEALASLSYKlg 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728   229 --TNTFRAINYVVAHVFKEESGARPDATKVLVIITDGEASDKGN-----ISAAHD--ITRYIIGIGKHFvsvqKQKTLHI 299
Cdd:smart00327  77 ggTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdllkaAKELKRsgVKVFVVGVGNDV----DEEELKK 152
                          170
                   ....*....|....*....
gi 568949728   300 FASEPVEEFVKILDTFEKL 318
Cdd:smart00327 153 LASAPGGVYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
152-309 2.73e-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  Cd Length: 161  Bit Score: 113.16  E-value: 2.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 152 VDLVFLFDGSQSLDRKDFEKILEFMKDVMRKLSN--TSYQFAAVQFSTDCRTEFTFLDYvkqnKNPDVLLGSVQPM---- 225
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIgpDKTRVGLVQYSDDVRVEFSLNDY----KSKDDLLKAVKNLkylg 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 226 FLLTNTFRAINYVVAHVFKeESGARPDATKVLVIITDGEASDKGNISAA------HDITRYIIGIGKHFvsvqkQKTLHI 299
Cdd:cd01450   77 GGGTNTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDGGDPKEAaaklkdEGIKVFVVGVGPAD-----EEELRE 150
                        170
                 ....*....|
gi 568949728 300 FASEPVEEFV 309
Cdd:cd01450  151 IASCPSERHV 160
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
152-315 2.51e-25

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  Cd Length: 164  Bit Score: 104.62  E-value: 2.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 152 VDLVFLFDGSQSLDRKDFEKILEFMKDVMRKL--SNTSYQFAAVQFSTDCRTEFTFLDYvkQNKnpDVLLGSVQPMFLL- 228
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLdiGPDGVRVGVVQYSDDPRTEFYLNTY--RSK--DDVLEAVKNLRYIg 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 229 --TNTFRAINYVVAHVFKEESGARPDATKVLVIITDGEASDKGNISAAHDITryiIGIGKHFVSVQKQ--KTLHIFASEP 304
Cdd:cd01472   77 ggTNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELKQ---AGIEVFAVGVKNAdeEELKQIASDP 153
                        170
                 ....*....|.
gi 568949728 305 VEEFVKILDTF 315
Cdd:cd01472  154 KELYVFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
153-315 4.01e-23

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  Cd Length: 164  Bit Score: 98.51  E-value: 4.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 153 DLVFLFDGSQSLDRKDFEKILEFMKDV--MRKLSNTSYQFAAVQFSTDCRTEFtfldYVKQNKNPDVLLGSVQPMFLL-- 228
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVveAFEIGPDGVQVGLVQYSDDPRTEF----DLNAYTSKEDVLAAIKNLPYKgg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 229 -TNTFRAINYVVAHVFKEESGARPDATKVLVIITDGEASDkgNISAAHDITR------YIIGIGKHFVSVQKQktlhiFA 301
Cdd:cd01482   78 nTRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQD--DVELPARVLRnlgvnvFAVGVKDADESELKM-----IA 150
                        170
                 ....*....|....
gi 568949728 302 SEPVEEFVKILDTF 315
Cdd:cd01482  151 SKPSETHVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
150-329 5.83e-21

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  Cd Length: 224  Bit Score: 93.60  E-value: 5.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 150 GKVDLVFLFDGSQSLDRKDFEKILEFMKDVMRKL--SNTSYQFAAVQFSTDCRTEFTFLDYvkqNKNPDVL--LGSVQPM 225
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLdvGPDATRVGLVQYSSTVKQEFPLGRF---KSKADLKraVRRMEYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 226 FLLTNTFRAINYVVAHVFKEESGARPDAT---KVLVIITDGEASDK-GNISA---AHDITRYIIGIGKHFVSvqkqkTLH 298
Cdd:cd01475   78 ETGTMTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDvSEVAAkarALGIEMFAVGVGRADEE-----ELR 152
                        170       180       190
                 ....*....|....*....|....*....|.
gi 568949728 299 IFASEPVEEFVKILDTFEKLKDLFTDLQRRI 329
Cdd:cd01475  153 EIASEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
152-285 3.54e-16

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  Cd Length: 161  Bit Score: 77.99  E-value: 3.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 152 VDLVFLFDGSQSLDRKDFEKILEFMKDVMRKLSNTS--YQFAAVQFSTDCRTEFTFLDYVKQNKNPDVLLGSVQPMFLLT 229
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949728 230 NTFRAINYVVAHVFKEesgARPDATKVLVIITDGEASDKGNISA-------AHDITRYIIGIG 285
Cdd:cd00198   81 NIGAALRLALELLKSA---KRPNARRVIILLTDGEPNDGPELLAeaarelrKLGITVYTIGIG 140
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
153-267 8.27e-13

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: 68.12  E-value: 8.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 153 DLVFLFDGSQSLDRKDFEKILEFMKDVMRKLS--NTSYQFAAVQFSTDCRTEFTFLDYvkQNKNPdvLLGSVQPMFLLT- 229
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTH--STKAD--VLGAVRRLRLRGg 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568949728 230 ---NTFRAINYVVAHVFKEESGARPD--ATKVLVIITDGEASD 267
Cdd:cd01481   78 sqlNTGSALDYVVKNLFTKSAGSRIEegVPQFLVLITGGKSQD 120
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
515-567 2.06e-11

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  Cd Length: 57  Bit Score: 61.62  E-value: 2.06e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568949728   515 PLGRFGAAITALTDINGDRLTDVAVGAPLE----EQGAVYIFNGKPGGLSPQPSQRI 567
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
610-740 2.68e-10

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: 312071  Cd Length: 447  Bit Score: 63.10  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728  610 SRPVVDVVTELSFSPEEIPVHEVECsysarEEQKHG----VKLKACFRI--KPLTPQfqgRLlaNLSYTLQLD---GHRM 680
Cdd:pfam08441   1 ARPVVNVNASLTVEPNSINLDKKNC-----TLPTGTpvscFTVRACFSYtgKPVYPP---SL--DLNYELELDslkKKGR 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568949728  681 RSRGLFPDG-SHELSGNTSITPDKS--CLDFHFHFPICIQDLISPINVSLNFSLLEEEGTPRD 740
Cdd:pfam08441  71 PPRVLFLDSqQPSLTTTLVLLSQGRkvCRDLTAYLRDNFRDKLTPIVIELNYSLRVPPRAKRA 133
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
153-284 5.35e-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  Cd Length: 163  Bit Score: 59.34  E-value: 5.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 153 DLVFLFDGSQSLDRKdFEKILEFMKDVMRKLSN--TSYQFAAVQFSTDCRT--EFTFLDYVKQNKnpdvLLGSVQPMFLL 228
Cdd:cd01476    2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIgpTATRVALITYSGRGRQrvRFNLPKHNDGEE----LLEKVDNLRFI 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568949728 229 ---TNTFRAINYVVAHvFKEESGARPDATKVLVIITDGEASDkgNISAAHDITRYIIGI 284
Cdd:cd01476   77 ggtTATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHD--DPEKQARILRAVPNI 132
VWA_2 pfam13519
von Willebrand factor type A domain;
154-264 6.89e-09

von Willebrand factor type A domain;


Pssm-ID: 316077  Cd Length: 107  Bit Score: 55.36  E-value: 6.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728  154 LVFLFDGSQSLDRKD-----FEKILEFMKDVMRKLSNTsyQFAAVQFSTDCRTEFTFldyvkqNKNPDVLLG---SVQPM 225
Cdd:pfam13519   1 LVFVVDTSGSMRNGDygptrLEAAKDAVNALLASLPGD--RVGLVTFGDGPEVLIPL------TKDRAKILRalrRLEPT 72
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568949728  226 FLLTNTFRAINYVVAHVFKEesgaRPDATKVLVIITDGE 264
Cdd:pfam13519  73 GGGTDLAAALQLARAALKHR----RKNQPRVIVLITDGE 107
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
150-294 1.62e-08

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757  Cd Length: 186  Bit Score: 55.08  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 150 GKVDLVFLFDGSQSLDRKDFEKILEFMKDVM--------RKLSNTSYQFAAVQFSTDCRTEFTFLDYVkqnKNPDVLLGS 221
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAerflkdyyRKDPAGSWRVGVVQYSDQQEVEAGFLRDI---RNYTSLKEA 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949728 222 VQPMFLL---TNTFRAINYVVAHVFKeesGARPDATKVLVIITDGE---ASDKGNISAAHDITRyiIGIGKHFVSVQKQ 294
Cdd:cd01480   78 VDNLEYIgggTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHsdgSPDGGIEKAVNEADH--LGIKIFFVAVGSQ 151
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
152-297 3.12e-07

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  Cd Length: 186  Bit Score: 51.23  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 152 VDLVFLFDGSQSLDRKD-FEKILEFMKDVMRKL--SNTSYQFAAVQFSTDCRTEFTFLDYVKQNKN-PDVLLGSVQPMFL 227
Cdd:cd01471    1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLniSPDEINLYLVTFSTNAKELIRLSSPNSTNKDlALNAIRALLSLYY 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568949728 228 ---LTNTFRAINYVVAHVFkEESGARPDATKVLVIITDGEASDKGN-ISAAHDITRY-----IIGIGkHFVSVQKQKTL 297
Cdd:cd01471   81 pngSTNTTSALLVVEKHLF-DTRGNRENAPQLVIIMTDGIPDSKFRtLKEARKLRERgviiaVLGVG-QGVNHEENRSL 157
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
150-319 1.53e-06

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  Cd Length: 185  Bit Score: 49.05  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 150 GKVDLVFLFDGSQSLDRKDFEkILEFMKDVMRKLSNTSYQFAAVQFSTDCRTEFTFLDYVKQNKNPDVLLGSVQPMFlLT 229
Cdd:cd01474    3 GHFDLYFVLDKSGSVAANWIE-IYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSG-QT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 230 NTFRAINYVVAHVFKEESGARPDAtKVLVIITDGEASDKGNISAAHDITR--------YIIGIgKHFvsvQKQKTLHIFA 301
Cdd:cd01474   81 YIHEGLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKYPEHEAKLsrklgaivYCVGV-TDF---LKSQLINIAD 155
                        170
                 ....*....|....*...
gi 568949728 302 SEpvEEFVKILDTFEKLK 319
Cdd:cd01474  156 SK--EYVFPVTSGFQALS 171
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
454-500 5.71e-05

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


Pssm-ID: 214549  Cd Length: 57  Bit Score: 42.75  E-value: 5.71e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568949728   454 IGSYFGGELCSV-DLDQDGEAELLlIGAPLFFGEQRGGRVFTYQRRQS 500
Cdd:smart00191   1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSG 47
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
519-552 8.38e-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: 307792  Cd Length: 36  Bit Score: 42.14  E-value: 8.38e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568949728  519 FGAAItALTDINGDRLTDVAVGAPL---EEQGAVYIF 552
Cdd:pfam01839   1 FGSSV-AVGDLNGDGYADLAVGAPAaggTGGGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
399-449 8.77e-05

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


Pssm-ID: 214549  Cd Length: 57  Bit Score: 42.36  E-value: 8.77e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568949728   399 GGYLGYTVAWMT--SRSSRPLLAAGAPRYQH---VGQVLLFQAPEAGGRWNQTQKI 449
Cdd:smart00191   2 GSYFGYSVAGVGdvNGDGYPDLLVGAPRANDageTGAVYVYFGSSGGGNSIPLQNL 57
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
152-286 2.50e-03

VWA BatA type: 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. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.


Pssm-ID: 238744  Cd Length: 180  Bit Score: 39.62  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568949728 152 VDLVFLFDGSQSLDRKDFEKI--LEFMKDVMRKLSN--TSYQFAAVQFSTDC--RTEFTfLDYVKQNKnpdvLLGSVQPM 225
Cdd:cd01467    3 RDIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFIDrrENDRIGLVVFAGAAftQAPLT-LDRESLKE----LLEDIKIG 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568949728 226 FLLTNTF--RAINYVVAHVFKEESGARpdatkVLVIITDGEaSDKGNIS--------AAHDITRYIIGIGK 286
Cdd:cd01467   78 LAGQGTAigDAIGLAIKRLKNSEAKER-----VIVLLTDGE-NNAGEIDpataaelaKNKGVRIYTIGVGK 142
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
578-622 9.72e-03

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  Cd Length: 57  Bit Score: 36.20  E-value: 9.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568949728   578 WFGRSIHGVKDLGGDRLADVVVGA--------EGRVVVLSSRPVVDVVTELSF 622
Cdd:smart00191   4 YFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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