NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564331001|ref|XP_006230331|]
View 

integrin alpha-L isoform X1 [Rattus norvegicus]

Protein Classification

VWA domain-containing protein( domain architecture ID 12192546)

VWA (von Willebrand factor type A) domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 151-320 4.37e-62

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: 469594 [Multi-domain]  Cd Length: 177  Bit Score: 209.13  E-value: 4.37e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  151 VDLVFLFDGSQSLDKKDFEKIVDFMKDVMRKLSN--TSYQFAAVQFSTECKTEFTFLDYIKlNKNPDVLLGNVTPMFLLT 228
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRT-KEEPLSLVKHISQLLGLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  229 NTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNG----NIDAA--QDITRYIIGIGKHFSTTQKQEKLHIFASK 302
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPllkdVIPQAerEGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 564331001  303 PVEEFVKILDTFEKLKDL 320
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 ...
 610-978 1.01e-36

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: 144.77  E-value: 1.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   610 RPVVDIVTELSFSPDEIPVHEVECSYSASQeqkegvklKVCFQIRpLTSQFQGRLLANLS----YTLQLD---GHRTRSR 682
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTP--------VSCFTVR-ACFSYTGKPIPNPSlvlnYELELDrqkKKGLPPR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   683 GLFpggsreLGGNTSVT---------PDKSCMDFHFHFPICIQDLISPINVSLNFSLLEeegSPRDQKGGRDMQPIL--- 750
Cdd:pfam08441   72 VLF------LDSQQPSLtgtlvllsqGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRV---DPRAPSDLPGLKPILdqn 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   751 RPSIhaVTKEIPFEKNCGEDKKCEADLALS----PPARSGVLRLMSSASLAVEWTLRNLGEDAYWVRLDLDFPRGLSFRK 826
Cdd:pfam08441  143 QPST--VQEQANFLKDCGEDNVCVPDLQLSakfdSRESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSG 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   827 VEMLQPHSQIpvSCEELTEESsllTKTLKCNVSSPiFKAGKQMTLQVMFNTLLNSSWGDFVELNGTVHCENENSSlgKDN 906
Cdd:pfam08441  221 VRREGSEKQL--SCTAKKENS---TRQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS--NSN 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   907 sattriPVLYPVNILTEDQ------ENSTLYISFTPKG-----PKT-----QQVQHIYKVRIQ-PSAydhnMPALEALVE 969
Cdd:pfam08441  293 ------PVSLKVPVVAEAQlslsgvSKPDQVVGGSVKGesamkPRSeedigPLVEHTYEVINNgPST----VSGASLEIS 362


                   ....*....
gi 564331001   970 VPQPHSEGP 978
Cdd:pfam08441  363 WPYELSNGK 371
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 514-566 7.92e-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: 63.93  E-value: 7.92e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 564331001    514 PLGRFGAAISALTDINGDGLTDVAVGAPLE----EQGAVYIFNGKPGGFSSQSSQRI 566
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 453-499 2.47e-07

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 48.53  E-value: 2.47e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 564331001    453 IGSYFGGELCSV-DLHQDGETDLLlIGAPLFYGEQRGGRVSVYQRRRS 499
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSG 47
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 398-448 1.76e-05

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 43.13  E-value: 1.76e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 564331001    398 GGYLGYTVAWLT--SRSSRPLLAAGAPRYQH---VGQVLLFQAPEAGGHWNQTQKI 448
Cdd:smart00191    2 GSYFGYSVAGVGdvNGDGYPDLLVGAPRANDageTGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 38-81 2.25e-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 [Multi-domain]  Cd Length: 57  Bit Score: 37.35  E-value: 2.25e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 564331001     38 AGRHFGYQVLQFGDG-------VVVGAPGEGNS--TGSLYHC--HPSSGSCQPVH 81
Cdd:smart00191    1 PGSYFGYSVAGVGDVngdgypdLLVGAPRANDAgeTGAVYVYfgSSGGGNSIPLQ 55
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 577-621 4.66e-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 [Multi-domain]  Cd Length: 57  Bit Score: 36.58  E-value: 4.66e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 564331001    577 WFGRSIHGVKDLGGDRLADVVVGA--------EGQVIVLSSRPVVDIVTELSF 621
Cdd:smart00191    4 YFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1109-1123 7.05e-03

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


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 35.17  E-value: 7.05e-03
                           10
                   ....*....|....*
gi 564331001  1109 KVGFFKRKLKEKMEA 1123
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 151-320 4.37e-62

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: 209.13  E-value: 4.37e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  151 VDLVFLFDGSQSLDKKDFEKIVDFMKDVMRKLSN--TSYQFAAVQFSTECKTEFTFLDYIKlNKNPDVLLGNVTPMFLLT 228
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRT-KEEPLSLVKHISQLLGLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  229 NTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNG----NIDAA--QDITRYIIGIGKHFSTTQKQEKLHIFASK 302
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPllkdVIPQAerEGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 564331001  303 PVEEFVKILDTFEKLKDL 320
Cdd:cd01469   160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
152-323 1.02e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.81  E-value: 1.02e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   152 DLVFLFDGSQSLDKKDFEKIVDFMKDVMRKL--SNTSYQFAAVQFSTECKTEFTFLDYiklnKNPDVLLGNVTPMFLL-- 227
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDY----SSKEELLSAVDNLRYLgg 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   228 --TNTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNGNIDAA-----QDITRYIIGIGKHFSttqkqEKLHIFA 300
Cdd:pfam00092   77 gtTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGDPEEVArelksAGVTVFAVGVGNADD-----EELRKIA 151

                          170       180
                   ....*....|....*....|...
gi 564331001   301 SKPVEEFVKILDTFEKLKDLFTD 323
Cdd:pfam00092  152 SEPGEGHVFTVSDFEALEDLQDQ 174
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 610-978 1.01e-36

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: 144.77  E-value: 1.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   610 RPVVDIVTELSFSPDEIPVHEVECSYSASQeqkegvklKVCFQIRpLTSQFQGRLLANLS----YTLQLD---GHRTRSR 682
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTP--------VSCFTVR-ACFSYTGKPIPNPSlvlnYELELDrqkKKGLPPR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   683 GLFpggsreLGGNTSVT---------PDKSCMDFHFHFPICIQDLISPINVSLNFSLLEeegSPRDQKGGRDMQPIL--- 750
Cdd:pfam08441   72 VLF------LDSQQPSLtgtlvllsqGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRV---DPRAPSDLPGLKPILdqn 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   751 RPSIhaVTKEIPFEKNCGEDKKCEADLALS----PPARSGVLRLMSSASLAVEWTLRNLGEDAYWVRLDLDFPRGLSFRK 826
Cdd:pfam08441  143 QPST--VQEQANFLKDCGEDNVCVPDLQLSakfdSRESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSG 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   827 VEMLQPHSQIpvSCEELTEESsllTKTLKCNVSSPiFKAGKQMTLQVMFNTLLNSSWGDFVELNGTVHCENENSSlgKDN 906
Cdd:pfam08441  221 VRREGSEKQL--SCTAKKENS---TRQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS--NSN 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   907 sattriPVLYPVNILTEDQ------ENSTLYISFTPKG-----PKT-----QQVQHIYKVRIQ-PSAydhnMPALEALVE 969
Cdd:pfam08441  293 ------PVSLKVPVVAEAQlslsgvSKPDQVVGGSVKGesamkPRSeedigPLVEHTYEVINNgPST----VSGASLEIS 362


                   ....*....
gi 564331001   970 VPQPHSEGP 978
Cdd:pfam08441  363 WPYELSNGK 371
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 152-317 1.10e-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 [Multi-domain]  Cd Length: 175  Bit Score: 116.40  E-value: 1.10e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001    152 DLVFLFDGSQSLDKKDFEKIVDFMKDVMRKL--SNTSYQFAAVQFSTECKTEFTFLDY-------IKLNKNPDVLLGNvt 222
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDSrskdallEALASLSYKLGGG-- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001    223 pmfllTNTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNGN-----IDAAQD--ITRYIIGIGKHFSttqkQEK 295
Cdd:smart00327   79 -----TNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdllkaAKELKRsgVKVFVVGVGNDVD----EEE 149

                           170       180
                    ....*....|....*....|..
gi 564331001    296 LHIFASKPVEEFVKILDTFEKL 317
Cdd:smart00327  150 LKKLASAPGGVYVFLPELLDLL 171
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 514-566 7.92e-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: 63.93  E-value: 7.92e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 564331001    514 PLGRFGAAISALTDINGDGLTDVAVGAPLE----EQGAVYIFNGKPGGFSSQSSQRI 566
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 518-551 2.03e-08

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: 50.97  E-value: 2.03e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 564331001   518 FGAAISAlTDINGDGLTDVAVGAPLE---EQGAVYIF 551
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEggaGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 453-499 2.47e-07

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 48.53  E-value: 2.47e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 564331001    453 IGSYFGGELCSV-DLHQDGETDLLlIGAPLFYGEQRGGRVSVYQRRRS 499
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSG 47
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 398-448 1.76e-05

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 43.13  E-value: 1.76e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 564331001    398 GGYLGYTVAWLT--SRSSRPLLAAGAPRYQH---VGQVLLFQAPEAGGHWNQTQKI 448
Cdd:smart00191    2 GSYFGYSVAGVGdvNGDGYPDLLVGAPRANDageTGAVYVYFGSSGGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 457-494 8.76e-04

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: 37.88  E-value: 8.76e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 564331001   457 FGGELCSVDLHQDGETDlLLIGAPlFYGEQRGGRVSVY 494
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAP-GEGGAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 38-81 2.25e-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 [Multi-domain]  Cd Length: 57  Bit Score: 37.35  E-value: 2.25e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 564331001     38 AGRHFGYQVLQFGDG-------VVVGAPGEGNS--TGSLYHC--HPSSGSCQPVH 81
Cdd:smart00191    1 PGSYFGYSVAGVGDVngdgypdLLVGAPRANDAgeTGAVYVYfgSSGGGNSIPLQ 55
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 577-621 4.66e-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 [Multi-domain]  Cd Length: 57  Bit Score: 36.58  E-value: 4.66e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 564331001    577 WFGRSIHGVKDLGGDRLADVVVGA--------EGQVIVLSSRPVVDIVTELSF 621
Cdd:smart00191    4 YFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1109-1123 7.05e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 35.17  E-value: 7.05e-03
                           10
                   ....*....|....*
gi 564331001  1109 KVGFFKRKLKEKMEA 1123
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
FG-GAP_2 pfam14312
FG-GAP repeat;
38-68 9.49e-03

FG-GAP repeat;


Pssm-ID: 316802 [Multi-domain]  Cd Length: 49  Bit Score: 35.19  E-value: 9.49e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 564331001    38 AGRHFGYQVLQFGDGVVVGAPGE---GNSTGSLY 68
Cdd:pfam14312   14 AGDYFGWSVAISGDTAVVGAYGDddnGSNSGSAY 47
 
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 ...
 151-320 4.37e-62

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: 209.13  E-value: 4.37e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  151 VDLVFLFDGSQSLDKKDFEKIVDFMKDVMRKLSN--TSYQFAAVQFSTECKTEFTFLDYIKlNKNPDVLLGNVTPMFLLT 228
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRT-KEEPLSLVKHISQLLGLT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  229 NTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNG----NIDAA--QDITRYIIGIGKHFSTTQKQEKLHIFASK 302
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPllkdVIPQAerEGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 564331001  303 PVEEFVKILDTFEKLKDL 320
Cdd:cd01469   160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
152-323 1.02e-40

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 147.81  E-value: 1.02e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   152 DLVFLFDGSQSLDKKDFEKIVDFMKDVMRKL--SNTSYQFAAVQFSTECKTEFTFLDYiklnKNPDVLLGNVTPMFLL-- 227
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDY----SSKEELLSAVDNLRYLgg 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   228 --TNTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNGNIDAA-----QDITRYIIGIGKHFSttqkqEKLHIFA 300
Cdd:pfam00092   77 gtTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGDPEEVArelksAGVTVFAVGVGNADD-----EELRKIA 151

                          170       180
                   ....*....|....*....|...
gi 564331001   301 SKPVEEFVKILDTFEKLKDLFTD 323
Cdd:pfam00092  152 SEPGEGHVFTVSDFEALEDLQDQ 174
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 610-978 1.01e-36

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: 144.77  E-value: 1.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   610 RPVVDIVTELSFSPDEIPVHEVECSYSASQeqkegvklKVCFQIRpLTSQFQGRLLANLS----YTLQLD---GHRTRSR 682
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTP--------VSCFTVR-ACFSYTGKPIPNPSlvlnYELELDrqkKKGLPPR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   683 GLFpggsreLGGNTSVT---------PDKSCMDFHFHFPICIQDLISPINVSLNFSLLEeegSPRDQKGGRDMQPIL--- 750
Cdd:pfam08441   72 VLF------LDSQQPSLtgtlvllsqGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRV---DPRAPSDLPGLKPILdqn 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   751 RPSIhaVTKEIPFEKNCGEDKKCEADLALS----PPARSGVLRLMSSASLAVEWTLRNLGEDAYWVRLDLDFPRGLSFRK 826
Cdd:pfam08441  143 QPST--VQEQANFLKDCGEDNVCVPDLQLSakfdSRESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSG 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   827 VEMLQPHSQIpvSCEELTEESsllTKTLKCNVSSPiFKAGKQMTLQVMFNTLLNSSWGDFVELNGTVHCENENSSlgKDN 906
Cdd:pfam08441  221 VRREGSEKQL--SCTAKKENS---TRQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS--NSN 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   907 sattriPVLYPVNILTEDQ------ENSTLYISFTPKG-----PKT-----QQVQHIYKVRIQ-PSAydhnMPALEALVE 969
Cdd:pfam08441  293 ------PVSLKVPVVAEAQlslsgvSKPDQVVGGSVKGesamkPRSeedigPLVEHTYEVINNgPST----VSGASLEIS 362


                   ....*....
gi 564331001   970 VPQPHSEGP 978
Cdd:pfam08441  363 WPYELSNGK 371
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 152-317 1.10e-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 [Multi-domain]  Cd Length: 175  Bit Score: 116.40  E-value: 1.10e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001    152 DLVFLFDGSQSLDKKDFEKIVDFMKDVMRKL--SNTSYQFAAVQFSTECKTEFTFLDY-------IKLNKNPDVLLGNvt 222
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDSrskdallEALASLSYKLGGG-- 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001    223 pmfllTNTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNGN-----IDAAQD--ITRYIIGIGKHFSttqkQEK 295
Cdd:smart00327   79 -----TNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdllkaAKELKRsgVKVFVVGVGNDVD----EEE 149

                           170       180
                    ....*....|....*....|..
gi 564331001    296 LHIFASKPVEEFVKILDTFEKL 317
Cdd:smart00327  150 LKKLASAPGGVYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 151-308 1.39e-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: 112.77  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  151 VDLVFLFDGSQSLDKKDFEKIVDFMKDVMRKLSN--TSYQFAAVQFSTECKTEFTFLDYiklnKNPDVLLGNVTPM---- 224
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIgpDKTRVGLVQYSDDVRVEFSLNDY----KSKDDLLKAVKNLkylg 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  225 FLLTNTFRAINYVVTHVFKeESGARPDATKVLVIITDGEASDNGNI-DAAQD-----ITRYIIGIGKHFsttqkQEKLHI 298
Cdd:cd01450    77 GGGTNTGKALQYALEQLFS-ESNARENVPKVIIVLTDGRSDDGGDPkEAAAKlkdegIKVFVVGVGPAD-----EEELRE 150

                         170
                  ....*....|
gi 564331001  299 FASKPVEEFV 308
Cdd:cd01450   151 IASCPSERHV 160
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 151-314 1.31e-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: 107.31  E-value: 1.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  151 VDLVFLFDGSQSLDKKDFEKIVDFMKDVMRKL--SNTSYQFAAVQFSTECKTEFTFLDYiklnKNPDVLLGNVTPMFLL- 227
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLdiGPDGVRVGVVQYSDDPRTEFYLNTY----RSKDDVLEAVKNLRYIg 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  228 --TNTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNGNIDAAQD----ITRYIIGIGKhfsttQKQEKLHIFAS 301
Cdd:cd01472    77 ggTNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELkqagIEVFAVGVKN-----ADEEELKQIAS 151

                         170
                  ....*....|...
gi 564331001  302 KPVEEFVKILDTF 314
Cdd:cd01472   152 DPKELYVFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 152-314 6.73e-24

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: 99.28  E-value: 6.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  152 DLVFLFDGSQSLDKKDFEKIVDFMKDV--MRKLSNTSYQFAAVQFSTECKTEFTfLDyiKLNKNPDVL--LGNVTPMFLL 227
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVveAFEIGPDGVQVGLVQYSDDPRTEFD-LN--AYTSKEDVLaaIKNLPYKGGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  228 TNTFRAINYVVTHVFKEESGARPDATKVLVIITDGEASDNGNIDA----AQDITRYIIGIGKHfsttqKQEKLHIFASKP 303
Cdd:cd01482    79 TRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELPArvlrNLGVNVFAVGVKDA-----DESELKMIASKP 153

                         170
                  ....*....|.
gi 564331001  304 VEEFVKILDTF 314
Cdd:cd01482   154 SETHVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 149-328 3.02e-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 [Multi-domain]  Cd Length: 224  Bit Score: 93.60  E-value: 3.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  149 GNVDLVFLFDGSQSLDKKDFEKIVDFMKDVMRKL--SNTSYQFAAVQFSTECKTEFTFLDYiklNKNPDVL--LGNVTPM 224
Cdd:cd01475     1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLdvGPDATRVGLVQYSSTVKQEFPLGRF---KSKADLKraVRRMEYL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  225 FLLTNTFRAINYVVTHVFKEESGARPDAT---KVLVIITDGEASDNGNIDAAQ----DITRYIIGIGKHFSTTQKQeklh 297
Cdd:cd01475    78 ETGTMTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKaralGIEMFAVGVGRADEEELRE---- 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 564331001  298 iFASKPVEEFVKILDTFEKLKDLFTDLQRKI 328
Cdd:cd01475   154 -IASEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 151-308 3.06e-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 [Multi-domain]  Cd Length: 161  Bit Score: 77.22  E-value: 3.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  151 VDLVFLFDGSQSLDKKDFEKIVDFMKDVMRKLSNTS--YQFAAVQFSTECKTEFTFLDYIKLNKNPDVLLGNVTPMFLLT 228
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  229 NTFRAINYVVTHVFKEesgARPDATKVLVIITDGEASDNGNIDA-------AQDITRYIIGIGkhfsTTQKQEKLHIFAS 301
Cdd:cd00198    81 NIGAALRLALELLKSA---KRPNARRVIILLTDGEPNDGPELLAeaarelrKLGITVYTIGIG----DDANEDELKEIAD 153


                  ....*..
gi 564331001  302 KPVEEFV 308
Cdd:cd00198   154 KTTGGAV 160
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 514-566 7.92e-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: 63.93  E-value: 7.92e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 564331001    514 PLGRFGAAISALTDINGDGLTDVAVGAPLE----EQGAVYIFNGKPGGFSSQSSQRI 566
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 152-266 2.23e-12

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: 66.19  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  152 DLVFLFDGSQSLDKKDFEKIVDFMKDVMRKLS--NTSYQFAAVQFSTECKTEFTFLDYiklnKNPDVLLGNVTPMFLLT- 228
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTH----STKADVLGAVRRLRLRGg 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 564331001  229 ---NTFRAINYVVTHVFKEESGARPD--ATKVLVIITDGEASD 266
Cdd:cd01481    78 sqlNTGSALDYVVKNLFTKSAGSRIEegVPQFLVLITGGKSQD 120
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 152-283 1.55e-11

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: 63.96  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  152 DLVFLFDGSQSLDKKdFEKIVDFMKDVMRKLSN--TSYQFAAVQFSTECKTEFTFldyiKLNKNPD--VLLGNVTPMFLL 227
Cdd:cd01476     2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEIgpTATRVALITYSGRGRQRVRF----NLPKHNDgeELLEKVDNLRFI 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564331001  228 ---TNTFRAINYVVTHvFKEESGARPDATKVLVIITDGEASDngNIDAAQDITRYIIGI 283
Cdd:cd01476    77 ggtTATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHD--DPEKQARILRAVPNI 132
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 149-303 3.58e-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: 57.40  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  149 GNVDLVFLFDGSQSLDKKDFEKIVDFMKDVM--------RKLSNTSYQFAAVQFSTECKTEFTFLDYIklnKNPDVLLGN 220
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAerflkdyyRKDPAGSWRVGVVQYSDQQEVEAGFLRDI---RNYTSLKEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  221 VTPMFLL---TNTFRAINYVVTHVFKeesGARPDATKVLVIITDGE---ASDNGNIDAAQDITRYIIGIGKHFSTTQKQE 294
Cdd:cd01480    78 VDNLEYIgggTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHsdgSPDGGIEKAVNEADHLGIKIFFVAVGSQNEE 154


                  ....*....
gi 564331001  295 KLHIFASKP 303
Cdd:cd01480   155 PLSRIACDG 163
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 518-551 2.03e-08

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: 50.97  E-value: 2.03e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 564331001   518 FGAAISAlTDINGDGLTDVAVGAPLE---EQGAVYIF 551
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEggaGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 453-499 2.47e-07

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 48.53  E-value: 2.47e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 564331001    453 IGSYFGGELCSV-DLHQDGETDLLlIGAPLFYGEQRGGRVSVYQRRRS 499
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSG 47
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 149-318 2.63e-07

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: 52.13  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  149 GNVDLVFLFDGSQSLDKKDFEkIVDFMKDVMRKLSNTSYQFAAVQFSTECKTEFTFLDYIKLNKNPDVLLGNVTPMFlLT 228
Cdd:cd01474     3 GHFDLYFVLDKSGSVAANWIE-IYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSG-QT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  229 NTFRAINYVVTHVFKEESGARPDAtKVLVIITDGEASDNGNIDAAQDITR--------YIIGIgKHFSttqKQEKLHIFA 300
Cdd:cd01474    81 YIHEGLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKYPEHEAKLsrklgaivYCVGV-TDFL---KSQLINIAD 155

                         170
                  ....*....|....*...
gi 564331001  301 SKpvEEFVKILDTFEKLK 318
Cdd:cd01474   156 SK--EYVFPVTSGFQALS 171
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 527-598 1.75e-05

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


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 43.37  E-value: 1.75e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331001   527 DINGDGLTDVAVGAPleEQGAVYIFNGKpGGFSSQSSQRIPGTQVSPGVRWFgrsihgvkDLGGDRLADVVV 598
Cdd:pfam13517    1 DLDGDGKLDLVVAND--GGLRLYLNNGD-GTFTFITSVSLGGGGGGLSVAVG--------DLDGDGRLDLLV 61
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 398-448 1.76e-05

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 43.13  E-value: 1.76e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 564331001    398 GGYLGYTVAWLT--SRSSRPLLAAGAPRYQH---VGQVLLFQAPEAGGHWNQTQKI 448
Cdd:smart00191    2 GSYFGYSVAGVGdvNGDGYPDLLVGAPRANDageTGAVYVYFGSSGGGNSIPLQNL 57
VWA_2 pfam13519
von Willebrand factor type A domain;
153-259 3.35e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 43.82  E-value: 3.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001   153 LVFLFDGSQSLDKKD-----FEKIVDFMKDVMRKLSNTsyQFAAVQFSTECKTEFTFldyiklNKNPDVLLG---NVTPM 224
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSLPGD--RVGLVTFGDGPEVLIPL------TKDRAKILRalrRLEPK 72

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 564331001   225 FLLTNTFRAINYVVTHVFKEesgaRPDATKVLVII 259
Cdd:pfam13519   73 GGGTNLAAALQLARAALKHR----RKNQPRRIVLI 103
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 151-266 4.63e-05

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: 45.45  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  151 VDLVFLFDGSQSLDKKD-FEKIVDFMKDVMRKL--SNTSYQFAAVQFSTECKTeftfldYIKLN----KNPDVLLGNVTP 223
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLniSPDEINLYLVTFSTNAKE------LIRLSspnsTNKDLALNAIRA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 564331001  224 MFLL------TNTFRAINYVVTHVFkEESGARPDATKVLVIITDGEASD 266
Cdd:cd01471    75 LLSLyypngsTNTTSALLVVEKHLF-DTRGNRENAPQLVIIMTDGIPDS 122
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 457-494 8.76e-04

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: 37.88  E-value: 8.76e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 564331001   457 FGGELCSVDLHQDGETDlLLIGAPlFYGEQRGGRVSVY 494
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAP-GEGGAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 38-81 2.25e-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 [Multi-domain]  Cd Length: 57  Bit Score: 37.35  E-value: 2.25e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 564331001     38 AGRHFGYQVLQFGDG-------VVVGAPGEGNS--TGSLYHC--HPSSGSCQPVH 81
Cdd:smart00191    1 PGSYFGYSVAGVGDVngdgypdLLVGAPRANDAgeTGAVYVYfgSSGGGNSIPLQ 55
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 151-319 2.34e-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 [Multi-domain]  Cd Length: 180  Bit Score: 40.39  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  151 VDLVFLFDGSQSLDKKDFEKI--VDFMKDVMRKLSN--TSYQFAAVQFSTECKTE--FTfLDYIKLNKnpdvLLGNVTPM 224
Cdd:cd01467     3 RDIMIALDVSGSMLAQDFVKPsrLEAAKEVLSDFIDrrENDRIGLVVFAGAAFTQapLT-LDRESLKE----LLEDIKIG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331001  225 FLLTNTF--RAINYVVTHVFKEESGARpdatkVLVIITDGEaSDNGNIDAAQ--------DITRYIIGIGKHFSttqkqe 294
Cdd:cd01467    78 LAGQGTAigDAIGLAIKRLKNSEAKER-----VIVLLTDGE-NNAGEIDPATaaelaknkGVRIYTIGVGKSGS------ 145

                         170       180
                  ....*....|....*....|....*
gi 564331001  295 klhifASKPVEEFVKILDTFEKLKD 319
Cdd:cd01467   146 -----GPKPDGSTILDEDSLVEIAD 165
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 577-621 4.66e-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 [Multi-domain]  Cd Length: 57  Bit Score: 36.58  E-value: 4.66e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 564331001    577 WFGRSIHGVKDLGGDRLADVVVGA--------EGQVIVLSSRPVVDIVTELSF 621
Cdd:smart00191    4 YFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1109-1123 7.05e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 35.17  E-value: 7.05e-03
                           10
                   ....*....|....*
gi 564331001  1109 KVGFFKRKLKEKMEA 1123
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
FG-GAP_2 pfam14312
FG-GAP repeat;
38-68 9.49e-03

FG-GAP repeat;


Pssm-ID: 316802 [Multi-domain]  Cd Length: 49  Bit Score: 35.19  E-value: 9.49e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 564331001    38 AGRHFGYQVLQFGDGVVVGAPGE---GNSTGSLY 68
Cdd:pfam14312   14 AGDYFGWSVAISGDTAVVGAYGDddnGSNSGSAY 47
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH