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Conserved domains on  [gi|530408048|ref|XP_005255370|]
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integrin alpha-L isoform X1 [Homo sapiens]

Protein Classification

VWA domain-containing protein( domain architecture ID 11546373)

VWA (von Willebrand factor type A) domain-containing protein similar to mammalian alpha subunits of integrins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 155-323 7.54e-80

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: 259.21  E-value: 7.54e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  155 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSN--TSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTN 232
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  233 TFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG----NIDAAK--DIIRYIIGIGKHFQTKESQETLHKFASKP 306
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPllkdVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                         170
                  ....*....|....*..
gi 530408048  307 ASEFVKILDTFEKLKDL 323
Cdd:cd01469   161 PEEHFFNVTDFAALKDI 177
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 613-998 2.65e-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: 143.62  E-value: 2.65e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   613 RPVVDMVTLMSFSPAEIPVHEVECSysTSNKMKEGVNITICFQIkSLIPQFQGRLVanLTYTLQLDghRTRRRGLFP--- 689
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCT--LTGTPVSCFTVRACFSY-TGKPIPNPSLV--LNYELELD--RQKKKGLPPrvl 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   690 ---GGRHELRRNIAVTTSMS--CTDFSFHFPVCVQDLISPINVSLNFSLweeegtPRDQRAGKDIPPiLRPSLH-----S 759
Cdd:pfam08441   74 fldSQQPSLTGTLVLLSQGRkvCRTTKAYLRDEFRDKLSPIVISLNYSL------RVDPRAPSDLPG-LKPILDqnqpsT 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   760 ETWEIPFEKNCGEDKKCEANLRVS----FSPARSRaLRLTAFASLSVELSLSNLEEDAYWVQLDLHFPPGLSFRKVEMLK 835
Cdd:pfam08441  147 VQEQANFLKDCGEDNVCVPDLQLSakfdSRESDEP-LLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREG 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   836 PHSQipVSCEELPEESrllSRALSCNVSSPiFKAGHSVALQMMFNTLVNSSWGDSVELHANVTCNNEDSDllEDNSATTI 915
Cdd:pfam08441  226 SEKQ--LSCTAKKENS---TRQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS--NSNPVSLK 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   916 IPILYPINILIQDQEDSTLYVSFTPKG-PKIH---------QVKHMYQVRIQ-PSihdhNIPTLEAVVGVPQPPSEGP-- 982
Cdd:pfam08441  298 VPVVAEAQLSLSGVSKPDQVVGGSVKGeSAMKprseedigpLVEHTYEVINNgPS----TVSGASLEISWPYELSNGKwl 373

                          410
                   ....*....|....*...
gi 530408048   983 --ITHqwsVQMEPPVPCH 998
Cdd:pfam08441  374 lyLLD---VQGQGKGECS 388
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-569 3.83e-13

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 65.09  E-value: 3.83e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 530408048    517 PLGRFGEAITALTDINGDGLVDVAVGAPLE----EQGAVYIFNGRHGGLSPQPSQRI 569
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 456-503 1.87e-08

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: 51.61  E-value: 1.87e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 530408048    456 IGSYFGGELCGV-DVDQDGETELLlIGAPLFYGEQRGGRVFIYQRRQLG 503
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1112-1126 2.72e-03

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


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.32  E-value: 2.72e-03
                           10
                   ....*....|....*
gi 530408048  1112 KVGFFKRNLKEKMEA 1126
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 579-603 3.89e-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: 3.89e-03
                            10        20
                    ....*....|....*....|....*
gi 530408048    579 QWFGRSIHGVKDLEGDGLADVAVGA 603
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 155-323 7.54e-80

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: 259.21  E-value: 7.54e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  155 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSN--TSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTN 232
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  233 TFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG----NIDAAK--DIIRYIIGIGKHFQTKESQETLHKFASKP 306
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPllkdVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                         170
                  ....*....|....*..
gi 530408048  307 ASEFVKILDTFEKLKDL 323
Cdd:cd01469   161 PEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
156-326 5.21e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 154.74  E-value: 5.21e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   156 DLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL--- 230
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDY---SSKEELLSAVDNLRYLggg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   231 -TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG---NIDAAKD--IIRYIIGIGKHfqtkeSQETLHKFAS 304
Cdd:pfam00092   78 tTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGDpeeVARELKSagVTVFAVGVGNA-----DDEELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 530408048   305 KPASEFVKILDTFEKLKDLFTE 326
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 613-998 2.65e-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: 143.62  E-value: 2.65e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   613 RPVVDMVTLMSFSPAEIPVHEVECSysTSNKMKEGVNITICFQIkSLIPQFQGRLVanLTYTLQLDghRTRRRGLFP--- 689
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCT--LTGTPVSCFTVRACFSY-TGKPIPNPSLV--LNYELELD--RQKKKGLPPrvl 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   690 ---GGRHELRRNIAVTTSMS--CTDFSFHFPVCVQDLISPINVSLNFSLweeegtPRDQRAGKDIPPiLRPSLH-----S 759
Cdd:pfam08441   74 fldSQQPSLTGTLVLLSQGRkvCRTTKAYLRDEFRDKLSPIVISLNYSL------RVDPRAPSDLPG-LKPILDqnqpsT 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   760 ETWEIPFEKNCGEDKKCEANLRVS----FSPARSRaLRLTAFASLSVELSLSNLEEDAYWVQLDLHFPPGLSFRKVEMLK 835
Cdd:pfam08441  147 VQEQANFLKDCGEDNVCVPDLQLSakfdSRESDEP-LLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREG 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   836 PHSQipVSCEELPEESrllSRALSCNVSSPiFKAGHSVALQMMFNTLVNSSWGDSVELHANVTCNNEDSDllEDNSATTI 915
Cdd:pfam08441  226 SEKQ--LSCTAKKENS---TRQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS--NSNPVSLK 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   916 IPILYPINILIQDQEDSTLYVSFTPKG-PKIH---------QVKHMYQVRIQ-PSihdhNIPTLEAVVGVPQPPSEGP-- 982
Cdd:pfam08441  298 VPVVAEAQLSLSGVSKPDQVVGGSVKGeSAMKprseedigpLVEHTYEVINNgPS----TVSGASLEISWPYELSNGKwl 373

                          410
                   ....*....|....*...
gi 530408048   983 --ITHqwsVQMEPPVPCH 998
Cdd:pfam08441  374 lyLLD---VQGQGKGECS 388
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 156-320 4.31e-34

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: 129.11  E-value: 4.31e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048    156 DLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL--- 230
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDS---RSKDALLEALASLSYKlgg 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048    231 -TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGN-----IDAAKD--IIRYIIGIGKHFQTKEsqetLHKF 302
Cdd:smart00327   78 gTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdllkaAKELKRsgVKVFVVGVGNDVDEEE----LKKL 153

                           170
                    ....*....|....*...
gi 530408048    303 ASKPASEFVKILDTFEKL 320
Cdd:smart00327  154 ASAPGGVYVFLPELLDLL 171
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-569 3.83e-13

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 65.09  E-value: 3.83e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 530408048    517 PLGRFGEAITALTDINGDGLVDVAVGAPLE----EQGAVYIFNGRHGGLSPQPSQRI 569
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 456-503 1.87e-08

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: 51.61  E-value: 1.87e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 530408048    456 IGSYFGGELCGV-DVDQDGETELLlIGAPLFYGEQRGGRVFIYQRRQLG 503
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 521-554 1.61e-07

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: 48.28  E-value: 1.61e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 530408048   521 FGEAItALTDINGDGLVDVAVGAPLE---EQGAVYIF 554
Cdd:pfam01839    1 FGYSV-AVGDLNGDGYADLAVGAPGEggaGAGAVYVL 36
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 155-327 1.69e-06

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 51.09  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  155 VDLVFLFD--GSMSLQPDefqkiLDFMKDVMKKLSNtSYQ----FAAVQFSTSYKTEFDFSDyvkrkDPDALLKHVKHML 228
Cdd:COG1240    93 RDVVLVVDasGSMAAENR-----LEAAKGALLDFLD-DYRprdrVGLVAFGGEAEVLLPLTR-----DREALKRALDELP 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  229 L--LTNTFGAInYVATEVFREElgaRPDATKVLIIITDGEATDSGN--IDAAKDIIR-----YIIGIGKhfqTKESQETL 299
Cdd:COG1240   162 PggGTPLGDAL-ALALELLKRA---DPARRKVIVLLTDGRDNAGRIdpLEAAELAAAagiriYTIGVGT---EAVDEGLL 234

                         170       180
                  ....*....|....*....|....*...
gi 530408048  300 HKFASKPASEFVKILDTfEKLKDLFTEL 327
Cdd:COG1240   235 REIAEATGGRYFRADDL-SELAAIYREI 261
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 460-497 4.61e-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: 38.65  E-value: 4.61e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 530408048   460 FGGELCGVDVDQDGETElLLIGAPlFYGEQRGGRVFIY 497
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAP-GEGGAGAGAVYVL 36
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 157-289 1.60e-03

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 41.91  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   157 LVFLFDGSMSLQPDefqkiLDFMKDVMKKLSNTSYQ----FAAVQFSTSYKTEFDFSDyvkrkDPDAL---LKHVKHMLL 229
Cdd:TIGR03436   56 VGLVIDTSGSMRND-----LDRARAAAIRFLKTVLRpndrVFVVTFNTRLRLLQDFTS-----DPRLLeaaLNRLKPPLR 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   230 L--------------TNTFGAINYVATEVFREELGARPDaTKVLIIITDGEATDSGN-----IDAAK--DIIRYIIGIGK 288
Cdd:TIGR03436  126 TdynssgafvrdgggTALYDAITLAALEQLANALAGIPG-RKALIVISDGGDNRSRDtleraIDAAQraDVAIYSIDARG 204


                   .
gi 530408048   289 H 289
Cdd:TIGR03436  205 L 205
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1112-1126 2.72e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.32  E-value: 2.72e-03
                           10
                   ....*....|....*
gi 530408048  1112 KVGFFKRNLKEKMEA 1126
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 579-603 3.89e-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: 3.89e-03
                            10        20
                    ....*....|....*....|....*
gi 530408048    579 QWFGRSIHGVKDLEGDGLADVAVGA 603
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 155-323 7.54e-80

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: 259.21  E-value: 7.54e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  155 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSN--TSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTN 232
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  233 TFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG----NIDAAK--DIIRYIIGIGKHFQTKESQETLHKFASKP 306
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPllkdVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                         170
                  ....*....|....*..
gi 530408048  307 ASEFVKILDTFEKLKDL 323
Cdd:cd01469   161 PEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
156-326 5.21e-43

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 154.74  E-value: 5.21e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   156 DLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL--- 230
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDY---SSKEELLSAVDNLRYLggg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   231 -TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSG---NIDAAKD--IIRYIIGIGKHfqtkeSQETLHKFAS 304
Cdd:pfam00092   78 tTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGDpeeVARELKSagVTVFAVGVGNA-----DDEELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 530408048   305 KPASEFVKILDTFEKLKDLFTE 326
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 613-998 2.65e-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: 143.62  E-value: 2.65e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   613 RPVVDMVTLMSFSPAEIPVHEVECSysTSNKMKEGVNITICFQIkSLIPQFQGRLVanLTYTLQLDghRTRRRGLFP--- 689
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCT--LTGTPVSCFTVRACFSY-TGKPIPNPSLV--LNYELELD--RQKKKGLPPrvl 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   690 ---GGRHELRRNIAVTTSMS--CTDFSFHFPVCVQDLISPINVSLNFSLweeegtPRDQRAGKDIPPiLRPSLH-----S 759
Cdd:pfam08441   74 fldSQQPSLTGTLVLLSQGRkvCRTTKAYLRDEFRDKLSPIVISLNYSL------RVDPRAPSDLPG-LKPILDqnqpsT 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   760 ETWEIPFEKNCGEDKKCEANLRVS----FSPARSRaLRLTAFASLSVELSLSNLEEDAYWVQLDLHFPPGLSFRKVEMLK 835
Cdd:pfam08441  147 VQEQANFLKDCGEDNVCVPDLQLSakfdSRESDEP-LLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREG 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   836 PHSQipVSCEELPEESrllSRALSCNVSSPiFKAGHSVALQMMFNTLVNSSWGDSVELHANVTCNNEDSDllEDNSATTI 915
Cdd:pfam08441  226 SEKQ--LSCTAKKENS---TRQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNS--NSNPVSLK 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   916 IPILYPINILIQDQEDSTLYVSFTPKG-PKIH---------QVKHMYQVRIQ-PSihdhNIPTLEAVVGVPQPPSEGP-- 982
Cdd:pfam08441  298 VPVVAEAQLSLSGVSKPDQVVGGSVKGeSAMKprseedigpLVEHTYEVINNgPS----TVSGASLEISWPYELSNGKwl 373

                          410
                   ....*....|....*...
gi 530408048   983 --ITHqwsVQMEPPVPCH 998
Cdd:pfam08441  374 lyLLD---VQGQGKGECS 388
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 155-311 3.53e-34

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: 128.95  E-value: 3.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  155 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSN--TSYQFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL-- 230
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIgpDKTRVGLVQYSDDVRVEFSLNDY---KSKDDLLKAVKNLKYLgg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  231 --TNTFGAINYVATEVFREElGARPDATKVLIIITDGEATDSGNIDAAKDIIR------YIIGIGKHfqtkeSQETLHKF 302
Cdd:cd01450    78 ggTNTGKALQYALEQLFSES-NARENVPKVIIVLTDGRSDDGGDPKEAAAKLKdegikvFVVGVGPA-----DEEELREI 151


                  ....*....
gi 530408048  303 ASKPASEFV 311
Cdd:cd01450   152 ASCPSERHV 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 156-320 4.31e-34

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: 129.11  E-value: 4.31e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048    156 DLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYvkrKDPDALLKHVKHMLLL--- 230
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDS---RSKDALLEALASLSYKlgg 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048    231 -TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGN-----IDAAKD--IIRYIIGIGKHFQTKEsqetLHKF 302
Cdd:smart00327   78 gTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdllkaAKELKRsgVKVFVVGVGNDVDEEE----LKKL 153

                           170
                    ....*....|....*...
gi 530408048    303 ASKPASEFVKILDTFEKL 320
Cdd:smart00327  154 ASAPGGVYVFLPELLDLL 171
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 155-317 4.47e-27

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: 108.47  E-value: 4.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  155 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYVKRKDpdaLLKHVKHMLLL-- 230
Cdd:cd01472     1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLdiGPDGVRVGVVQYSDDPRTEFYLNTYRSKDD---VLEAVKNLRYIgg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  231 -TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGNIDAAKD----IIRYIIGIGKHfqtkeSQETLHKFASK 305
Cdd:cd01472    78 gTNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELkqagIEVFAVGVKNA-----DEEELKQIASD 152

                         170
                  ....*....|..
gi 530408048  306 PASEFVKILDTF 317
Cdd:cd01472   153 PKELYVFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 156-317 1.22e-26

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 107.37  E-value: 1.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  156 DLVFLFDGSMSLQPDEFQKILDFMKDVMK--KLSNTSYQFAAVQFSTSYKTEFDFSDYVKRKDpdaLLKHVKHMLLL--- 230
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEafEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKED---VLAAIKNLPYKggn 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  231 TNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDsgNIDAAKDIIR------YIIGIGKHfqtkeSQETLHKFAS 304
Cdd:cd01482    79 TRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQD--DVELPARVLRnlgvnvFAVGVKDA-----DESELKMIAS 151

                         170
                  ....*....|...
gi 530408048  305 KPASEFVKILDTF 317
Cdd:cd01482   152 KPSETHVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 153-331 4.31e-25

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: 104.77  E-value: 4.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  153 GNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLL 230
Cdd:cd01475     1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLdvGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  231 TNTFGAINYVATEVFREELGARPDAT---KVLIIITDGEATDSGNIDAAK----DIIRYIIGIGkhfqtKESQETLHKFA 303
Cdd:cd01475    81 TMTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKaralGIEMFAVGVG-----RADEEELREIA 155

                         170       180
                  ....*....|....*....|....*...
gi 530408048  304 SKPASEFVKILDTFEKLKDLFTELQKKI 331
Cdd:cd01475   156 SEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 155-311 3.84e-17

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: 79.92  E-value: 3.84e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  155 VDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSNTS--YQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLL-LT 231
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGgGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  232 NTFGAINYVATEVFREelgARPDATKVLIIITDGEATDSGN-----IDAAKD--IIRYIIGIGKHFQTKEsqetLHKFAS 304
Cdd:cd00198    81 NIGAALRLALELLKSA---KRPNARRVIILLTDGEPNDGPEllaeaARELRKlgITVYTIGIGDDANEDE----LKEIAD 153


                  ....*..
gi 530408048  305 KPASEFV 311
Cdd:cd00198   154 KTTGGAV 160
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 156-270 1.95e-14

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: 72.36  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  156 DLVFLFDGSMSLQPDEFQKILDFMKDVMKKLS--NTSYQFAAVQFSTSYKTEFDFSDYVKRKDpdaLLKHVKHMLLLT-- 231
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTHSTKAD---VLGAVRRLRLRGgs 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 530408048  232 --NTFGAINYVATEVFREELGARPD--ATKVLIIITDGEATDS 270
Cdd:cd01481    79 qlNTGSALDYVVKNLFTKSAGSRIEegVPQFLVLITGGKSQDD 121
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-569 3.83e-13

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 65.09  E-value: 3.83e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 530408048    517 PLGRFGEAITALTDINGDGLVDVAVGAPLE----EQGAVYIFNGRHGGLSPQPSQRI 569
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 156-310 5.29e-12

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: 65.11  E-value: 5.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  156 DLVFLFDGSMSLQpDEFQKILDFMKDVMKKLSN--TSYQFAAVQFSTSYKT--EFDFSDYVKRKDPDALLKHVKHMLLLT 231
Cdd:cd01476     2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIgpTATRVALITYSGRGRQrvRFNLPKHNDGEELLEKVDNLRFIGGTT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  232 NTFGAINYvATEVFREELGARPDATKVLIIITDGEATDsgNIDAAKDIIR-----YIIGIGKHFQTKESQETLHKFASKP 306
Cdd:cd01476    81 ATGAAIEV-ALQQLDPSEGRREGIPKVVVVLTDGRSHD--DPEKQARILRavpniETFAVGTGDPGTVDTEELHSITGNE 157


                  ....
gi 530408048  307 ASEF 310
Cdd:cd01476   158 DHIF 161
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 456-503 1.87e-08

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: 51.61  E-value: 1.87e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 530408048    456 IGSYFGGELCGV-DVDQDGETELLlIGAPLFYGEQRGGRVFIYQRRQLG 503
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 521-554 1.61e-07

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: 48.28  E-value: 1.61e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 530408048   521 FGEAItALTDINGDGLVDVAVGAPLE---EQGAVYIF 554
Cdd:pfam01839    1 FGYSV-AVGDLNGDGYADLAVGAPGEggaGAGAVYVL 36
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 153-330 4.02e-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: 51.74  E-value: 4.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  153 GNVDLVFLFDGSMSLQpDEFQKILDFMKDVMKKLSNTSYQFAAVQFSTSYKTEFDFSDYvkRKDPDALLKHVKHMLL--L 230
Cdd:cd01474     3 GHFDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDD--SSAIIKGLEVLKKVTPsgQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  231 TNTFGAINYVATEVFREELGARPDAtKVLIIITDGEATDSGNIDAAKD--------IIRYIIGIgkhfqTKESQETLHKF 302
Cdd:cd01474    80 TYIHEGLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKYPEHEaklsrklgAIVYCVGV-----TDFLKSQLINI 153

                         170       180
                  ....*....|....*....|....*...
gi 530408048  303 ASKPASEFvKILDTFEKLKDLFTELQKK 330
Cdd:cd01474   154 ADSKEYVF-PVTSGFQALSGIIESVVKK 180
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 153-278 5.38e-07

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: 51.23  E-value: 5.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  153 GNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLS--------NTSYQFAAVQFSTSYKTEFDFSDYVkrKDPDALLKHV 224
Cdd:cd01480     1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLkdyyrkdpAGSWRVGVVQYSDQQEVEAGFLRDI--RNYTSLKEAV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  225 KHMLLL---TNTFGAINYVaTEVFREelGARPDATKVLIIITDGE---ATDSGNIDAAKD 278
Cdd:cd01480    79 DNLEYIgggTFTDCALKYA-TEQLLE--GSHQKENKFLLVITDGHsdgSPDGGIEKAVNE 135
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 155-287 1.13e-06

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 50.08  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  155 VDLVFLFDGSMSL-QPDEFQKILDFMKDVMKKL--SNTSYQFAAVQFSTSYKTEFDFSDYvKRKDPDALLKHVKHMLLL- 230
Cdd:cd01471     1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLniSPDEINLYLVTFSTNAKELIRLSSP-NSTNKDLALNAIRALLSLy 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530408048  231 -----TNTFGAINYVATEVFrEELGARPDATKVLIIITDGEA-TDSGNIDAAKDI-----IRYIIGIG 287
Cdd:cd01471    80 ypngsTNTTSALLVVEKHLF-DTRGNRENAPQLVIIMTDGIPdSKFRTLKEARKLrergvIIAVLGVG 146
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 155-327 1.69e-06

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 51.09  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  155 VDLVFLFD--GSMSLQPDefqkiLDFMKDVMKKLSNtSYQ----FAAVQFSTSYKTEFDFSDyvkrkDPDALLKHVKHML 228
Cdd:COG1240    93 RDVVLVVDasGSMAAENR-----LEAAKGALLDFLD-DYRprdrVGLVAFGGEAEVLLPLTR-----DREALKRALDELP 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  229 L--LTNTFGAInYVATEVFREElgaRPDATKVLIIITDGEATDSGN--IDAAKDIIR-----YIIGIGKhfqTKESQETL 299
Cdd:COG1240   162 PggGTPLGDAL-ALALELLKRA---DPARRKVIVLLTDGRDNAGRIdpLEAAELAAAagiriYTIGVGT---EAVDEGLL 234

                         170       180
                  ....*....|....*....|....*...
gi 530408048  300 HKFASKPASEFVKILDTfEKLKDLFTEL 327
Cdd:COG1240   235 REIAEATGGRYFRADDL-SELAAIYREI 261
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 530-601 5.66e-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: 41.83  E-value: 5.66e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530408048   530 DINGDGLVDVAVGAPleEQGAVYIFNGrhgglspqpsqriEGTQVLSGIQWFGRSIHG----VKDLEGDGLADVAV 601
Cdd:pfam13517    1 DLDGDGKLDLVVAND--GGLRLYLNNG-------------DGTFTFITSVSLGGGGGGlsvaVGDLDGDGRLDLLV 61
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 460-497 4.61e-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: 38.65  E-value: 4.61e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 530408048   460 FGGELCGVDVDQDGETElLLIGAPlFYGEQRGGRVFIY 497
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAP-GEGGAGAGAVYVL 36
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 157-289 1.60e-03

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 41.91  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   157 LVFLFDGSMSLQPDefqkiLDFMKDVMKKLSNTSYQ----FAAVQFSTSYKTEFDFSDyvkrkDPDAL---LKHVKHMLL 229
Cdd:TIGR03436   56 VGLVIDTSGSMRND-----LDRARAAAIRFLKTVLRpndrVFVVTFNTRLRLLQDFTS-----DPRLLeaaLNRLKPPLR 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048   230 L--------------TNTFGAINYVATEVFREELGARPDaTKVLIIITDGEATDSGN-----IDAAK--DIIRYIIGIGK 288
Cdd:TIGR03436  126 TdynssgafvrdgggTALYDAITLAALEQLANALAGIPG-RKALIVISDGGDNRSRDtleraIDAAQraDVAIYSIDARG 204


                   .
gi 530408048   289 H 289
Cdd:TIGR03436  205 L 205
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 468-541 1.84e-03

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


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 37.59  E-value: 1.84e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530408048   468 DVDQDGETELLLIGAplfygeqrgGRVFIYQRRQLG-FEEVSELQGDPGYplgrFGEAITALtDINGDGLVDVAV 541
Cdd:pfam13517    1 DLDGDGKLDLVVAND---------GGLRLYLNNGDGtFTFITSVSLGGGG----GGLSVAVG-DLDGDGRLDLLV 61
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
154-324 2.43e-03

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 40.68  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  154 NVDLVFLFD--GSMSLQP-----DEFQKILD-FMKDvmkKLSNTSYQFAAVQFSTSYKTEFDFSDYVKRKDPDallkhvk 225
Cdd:COG4245     5 RLPVYLLLDtsGSMSGEPiealnEGLQALIDeLRQD---PYALETVEVSVITFDGEAKVLLPLTDLEDFQPPD------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408048  226 hmlL----LTNTFGAINYVATEVFREELGARPDAT----KVLIIITDGEATDSG---------NIDAAKDIIRYIIGIGk 288
Cdd:COG4245    75 ---LsasgGTPLGAALELLLDLIERRVQKYTAEGKgdwrPVVFLITDGEPTDSDweaalqrlkDGEAAKKANIFAIGVG- 150

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 530408048  289 hfqTKESQETLHKFASKpasefVKILDT--FEKLKDLF 324
Cdd:COG4245   151 ---PDADTEVLKQLTDP-----VRALDAldGLDFREFF 180
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1112-1126 2.72e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.32  E-value: 2.72e-03
                           10
                   ....*....|....*
gi 530408048  1112 KVGFFKRNLKEKMEA 1126
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 579-603 3.89e-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: 3.89e-03
                            10        20
                    ....*....|....*....|....*
gi 530408048    579 QWFGRSIHGVKDLEGDGLADVAVGA 603
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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