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Conserved domains on  [gi|164565428|ref|NP_001101169|]
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integrin alpha-10 precursor [Rattus norvegicus]

Protein Classification

integrin alpha( domain architecture ID 12192535)

integrin alpha forms a heterodimer with integrin beta to mediate cell-extracellular matrix and cell-cell interactions; integrin alpha is a component of integrin, a cell adhesion molecule that mediates cell-extracellular matrix and cell-cell interactions

Gene Ontology:  GO:0007155|GO:0008305|GO:0005178|GO:0046872
PubMed:  3028640|2199285|12297042|12826403|14689578|12361595|12234368

Graphical summary

 Zoom to residue level

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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 ...
 166-346 5.17e-87

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


:

Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 278.86  E-value: 5.17e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  166 MDVVIVLDGSNSIYP--WSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGReT 243
Cdd:cd01469     1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  244 RTAQAIMVACTEGFSESRGGRPEAARLLVVVTDGESHDGEELPAALKACEAGRVTRYGIAVLGHYLRRqrdpsSFLREIR 323
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQRE-----NSREELK 154

                         170       180
                  ....*....|....*....|...
gi 164565428  324 AIASDPDERFFFNVTDEAALTDI 346
Cdd:cd01469   155 TIASKPPEEHFFNVTDFAALKDI 177
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 643-1050 1.49e-33

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: 135.53  E-value: 1.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   643 QPIIHLIPTLDVMPPHISVVQKDCKRRGQEAACLTASLCFQVKsqtpGRWDRRFHIRFSASLD-EWT----AGARAAFDG 717
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFSYT----GKPIPNPSLVLNYELElDRQkkkgLPPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   718 SGQRLSPGQLRL-SVGNVTCEQLHFHALDTS-DYLRPVALTVTFALDNTTKPG-------PVLAEGSSTSIRKLIPFSKD 788
Cdd:pfam08441   77 SQQPSLTGTLVLlSQGRKVCRTTKAYLRDEFrDKLSPIVISLNYSLRVDPRAPsdlpglkPILDQNQPSTVQEQANFLKD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   789 CGPDNECITDLVLQADMDIRGSRKsPFVVqGGRQKVLVSVTLENKKENAYNTSLSLSFSRNLHLASLTPQrAKSVKVECA 868
Cdd:pfam08441  157 CGEDNVCVPDLQLSAKFDSRESDE-PLLL-GDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRRE-GSEKQLSCT 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   869 VPSPHAR---LCIVGHPvFQAGAKVSFLLEFEFS-CTFLLSQVSVRLTASSSSLERNetlQDNTAQTSAYIRYEPHLMFS 944
Cdd:pfam08441  234 AKKENSTrqvVCDLGNP-MKRGTQVTFGLRFSVSgLELSTEELSFDLQIRSTNEQNS---NSNPVSLKVPVVAEAQLSLS 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   945 SEStlhryevHPYRAlpVGP----------------GPEFKTTLRVQNLGCHVVSGLVVSALLPAVAHGGNYFLSLSQV- 1007
Cdd:pfam08441  310 GVS-------KPDQV--VGGsvkgesamkprseediGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGKWLLYLLDVq 380

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164565428  1008 ISGNASCTVQNLTDP-----------------PGFPVHPEELQHTSR--------LN-GSNTRCQAVRC 1050
Cdd:pfam08441  381 GQGKGECSPQNEINPlnltqslesskplrtsrVHHVVKRRDVLKSEKatqtasvlLScDSGARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 545-599 2.03e-12

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: 62.78  E-value: 2.03e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 164565428    545 QDSRFGFAMAALPDLNHDGFSDVAVGAPLED--GHQGALYLYHGTQTGIRPHPTQRI 599
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANdaGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 482-525 1.39e-04

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 40.82  E-value: 1.39e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 164565428    482 IGSYFGSELCPL-DTDMDGITNiLLVAAPMflGPQNKETGRIYVY 525
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPR--ANDAGETGAVYVY 42
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 41-81 5.17e-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: 36.20  E-value: 5.17e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 164565428     41 FGYSVLQHV---GGGQRWMLVGAPWDGPSGdRKGDVYRCSIGGF 81
Cdd:smart00191    5 FGYSVAGVGdvnGDGYPDLLVGAPRANDAG-ETGAVYVYFGSSG 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 ...
 166-346 5.17e-87

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 278.86  E-value: 5.17e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  166 MDVVIVLDGSNSIYP--WSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGReT 243
Cdd:cd01469     1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  244 RTAQAIMVACTEGFSESRGGRPEAARLLVVVTDGESHDGEELPAALKACEAGRVTRYGIAVLGHYLRRqrdpsSFLREIR 323
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQRE-----NSREELK 154

                         170       180
                  ....*....|....*....|...
gi 164565428  324 AIASDPDERFFFNVTDEAALTDI 346
Cdd:cd01469   155 TIASKPPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
167-349 1.98e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 178.62  E-value: 1.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   167 DVVIVLDGSNSI--YPWSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGRETR 244
Cdd:pfam00092    1 DIVFLLDGSGSIggDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   245 TAQAIMVACTEGFSESRGGRPEAARLLVVVTDGESHDGEELPAALKACEAGrVTRYGIAVLGHYlrrqrdpssfLREIRA 324
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGDPEEVARELKSAG-VTVFAVGVGNAD----------DEELRK 149

                          170       180
                   ....*....|....*....|....*
gi 164565428   325 IASDPDERFFFNVTDEAALTDIVDA 349
Cdd:pfam00092  150 IASEPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 167-347 1.63e-38

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: 141.82  E-value: 1.63e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428    167 DVVIVLDGSNSIYP--WSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGRETR 244
Cdd:smart00327    1 DVVFLLDGSGSMGGnrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428    245 TAQAIMVACTEGFSESRGGRPEAARLLVVVTDGESHDGEE--LPAALKACEAGrVTRYGIAVLGHYLRrqrdpssflREI 322
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdlLKAAKELKRSG-VKVFVVGVGNDVDE---------EEL 150

                           170       180
                    ....*....|....*....|....*
gi 164565428    323 RAIASDPDERFFFNVTDEAALTDIV 347
Cdd:smart00327  151 KKLASAPGGVYVFLPELLDLLIDLL 175
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 643-1050 1.49e-33

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: 135.53  E-value: 1.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   643 QPIIHLIPTLDVMPPHISVVQKDCKRRGQEAACLTASLCFQVKsqtpGRWDRRFHIRFSASLD-EWT----AGARAAFDG 717
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFSYT----GKPIPNPSLVLNYELElDRQkkkgLPPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   718 SGQRLSPGQLRL-SVGNVTCEQLHFHALDTS-DYLRPVALTVTFALDNTTKPG-------PVLAEGSSTSIRKLIPFSKD 788
Cdd:pfam08441   77 SQQPSLTGTLVLlSQGRKVCRTTKAYLRDEFrDKLSPIVISLNYSLRVDPRAPsdlpglkPILDQNQPSTVQEQANFLKD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   789 CGPDNECITDLVLQADMDIRGSRKsPFVVqGGRQKVLVSVTLENKKENAYNTSLSLSFSRNLHLASLTPQrAKSVKVECA 868
Cdd:pfam08441  157 CGEDNVCVPDLQLSAKFDSRESDE-PLLL-GDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRRE-GSEKQLSCT 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   869 VPSPHAR---LCIVGHPvFQAGAKVSFLLEFEFS-CTFLLSQVSVRLTASSSSLERNetlQDNTAQTSAYIRYEPHLMFS 944
Cdd:pfam08441  234 AKKENSTrqvVCDLGNP-MKRGTQVTFGLRFSVSgLELSTEELSFDLQIRSTNEQNS---NSNPVSLKVPVVAEAQLSLS 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   945 SEStlhryevHPYRAlpVGP----------------GPEFKTTLRVQNLGCHVVSGLVVSALLPAVAHGGNYFLSLSQV- 1007
Cdd:pfam08441  310 GVS-------KPDQV--VGGsvkgesamkprseediGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGKWLLYLLDVq 380

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164565428  1008 ISGNASCTVQNLTDP-----------------PGFPVHPEELQHTSR--------LN-GSNTRCQAVRC 1050
Cdd:pfam08441  381 GQGKGECSPQNEINPlnltqslesskplrtsrVHHVVKRRDVLKSEKatqtasvlLScDSGARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 545-599 2.03e-12

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: 62.78  E-value: 2.03e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 164565428    545 QDSRFGFAMAALPDLNHDGFSDVAVGAPLED--GHQGALYLYHGTQTGIRPHPTQRI 599
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANdaGETGAVYVYFGSSGGGNSIPLQNL 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 145-351 1.03e-08

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 57.64  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  145 VDASFRLQGSLAPTAQRCPTYMDVVIVLDGSNSIY---PWSEVQTFLRRLVGRLfidPEQIQVGLVQYGENPvhEWSLGD 221
Cdd:COG1240    72 VLLLLLALALAPLALARPQRGRDVVLVVDASGSMAaenRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEA--EVLLPL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  222 FRTKEEVVRAARNLSRREGreTRTAQAIMVACTEGfsesRGGRPEAARLLVVVTDGESHDG-EELPAALKACEAGRVTRY 300
Cdd:COG1240   147 TRDREALKRALDELPPGGG--TPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGrIDPLEAAELAAAAGIRIY 220

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 164565428  301 GIAVLGHYLRRQrdpssFLREIrAIASDPDerfFFNVTDEAALTDIVDALG 351
Cdd:COG1240   221 TIGVGTEAVDEG-----LLREI-AEATGGR---YFRADDLSELAAIYREID 262
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 549-584 1.25e-06

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: 45.96  E-value: 1.25e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 164565428   549 FGFAMAALpDLNHDGFSDVAVGAPLEDG-HQGALYLY 584
Cdd:pfam01839    1 FGYSVAVG-DLNGDGYADLAVGAPGEGGaGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 482-525 1.39e-04

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 40.82  E-value: 1.39e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 164565428    482 IGSYFGSELCPL-DTDMDGITNiLLVAAPMflGPQNKETGRIYVY 525
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPR--ANDAGETGAVYVY 42
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 41-81 5.17e-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: 36.20  E-value: 5.17e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 164565428     41 FGYSVLQHV---GGGQRWMLVGAPWDGPSGdRKGDVYRCSIGGF 81
Cdd:smart00191    5 FGYSVAGVGdvnGDGYPDLLVGAPRANDAG-ETGAVYVYFGSSG 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 ...
 166-346 5.17e-87

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 278.86  E-value: 5.17e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  166 MDVVIVLDGSNSIYP--WSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGReT 243
Cdd:cd01469     1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  244 RTAQAIMVACTEGFSESRGGRPEAARLLVVVTDGESHDGEELPAALKACEAGRVTRYGIAVLGHYLRRqrdpsSFLREIR 323
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQRE-----NSREELK 154

                         170       180
                  ....*....|....*....|...
gi 164565428  324 AIASDPDERFFFNVTDEAALTDI 346
Cdd:cd01469   155 TIASKPPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
167-349 1.98e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 178.62  E-value: 1.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   167 DVVIVLDGSNSI--YPWSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGRETR 244
Cdd:pfam00092    1 DIVFLLDGSGSIggDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   245 TAQAIMVACTEGFSESRGGRPEAARLLVVVTDGESHDGEELPAALKACEAGrVTRYGIAVLGHYlrrqrdpssfLREIRA 324
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDGDPEEVARELKSAG-VTVFAVGVGNAD----------DEELRK 149

                          170       180
                   ....*....|....*....|....*
gi 164565428   325 IASDPDERFFFNVTDEAALTDIVDA 349
Cdd:pfam00092  150 IASEPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 167-347 1.63e-38

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: 141.82  E-value: 1.63e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428    167 DVVIVLDGSNSIYP--WSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGRETR 244
Cdd:smart00327    1 DVVFLLDGSGSMGGnrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428    245 TAQAIMVACTEGFSESRGGRPEAARLLVVVTDGESHDGEE--LPAALKACEAGrVTRYGIAVLGHYLRrqrdpssflREI 322
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKdlLKAAKELKRSG-VKVFVVGVGNDVDE---------EEL 150

                           170       180
                    ....*....|....*....|....*
gi 164565428    323 RAIASDPDERFFFNVTDEAALTDIV 347
Cdd:smart00327  151 KKLASAPGGVYVFLPELLDLLIDLL 175
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 643-1050 1.49e-33

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: 135.53  E-value: 1.49e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   643 QPIIHLIPTLDVMPPHISVVQKDCKRRGQEAACLTASLCFQVKsqtpGRWDRRFHIRFSASLD-EWT----AGARAAFDG 717
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFSYT----GKPIPNPSLVLNYELElDRQkkkgLPPRVLFLD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   718 SGQRLSPGQLRL-SVGNVTCEQLHFHALDTS-DYLRPVALTVTFALDNTTKPG-------PVLAEGSSTSIRKLIPFSKD 788
Cdd:pfam08441   77 SQQPSLTGTLVLlSQGRKVCRTTKAYLRDEFrDKLSPIVISLNYSLRVDPRAPsdlpglkPILDQNQPSTVQEQANFLKD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   789 CGPDNECITDLVLQADMDIRGSRKsPFVVqGGRQKVLVSVTLENKKENAYNTSLSLSFSRNLHLASLTPQrAKSVKVECA 868
Cdd:pfam08441  157 CGEDNVCVPDLQLSAKFDSRESDE-PLLL-GDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRRE-GSEKQLSCT 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   869 VPSPHAR---LCIVGHPvFQAGAKVSFLLEFEFS-CTFLLSQVSVRLTASSSSLERNetlQDNTAQTSAYIRYEPHLMFS 944
Cdd:pfam08441  234 AKKENSTrqvVCDLGNP-MKRGTQVTFGLRFSVSgLELSTEELSFDLQIRSTNEQNS---NSNPVSLKVPVVAEAQLSLS 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   945 SEStlhryevHPYRAlpVGP----------------GPEFKTTLRVQNLGCHVVSGLVVSALLPAVAHGGNYFLSLSQV- 1007
Cdd:pfam08441  310 GVS-------KPDQV--VGGsvkgesamkprseediGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGKWLLYLLDVq 380

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164565428  1008 ISGNASCTVQNLTDP-----------------PGFPVHPEELQHTSR--------LN-GSNTRCQAVRC 1050
Cdd:pfam08441  381 GQGKGECSPQNEINPlnltqslesskplrtsrVHHVVKRRDVLKSEKatqtasvlLScDSGARCVVIRC 449
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 166-335 5.25e-32

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: 122.40  E-value: 5.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  166 MDVVIVLDGSNSIYP--WSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGRET 243
Cdd:cd01450     1 LDIVFLLDGSESVGPenFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  244 RTAQAIMVAcTEGFSESRGGRPEAARLLVVVTDGESHDGEELPAALKACEAGRVTRYGIAVLGHYlrrqrdpssfLREIR 323
Cdd:cd01450    81 NTGKALQYA-LEQLFSESNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGVGPAD----------EEELR 149

                         170
                  ....*....|..
gi 164565428  324 AIASDPDERFFF 335
Cdd:cd01450   150 EIASCPSERHVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 167-339 1.10e-31

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: 121.62  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  167 DVVIVLDGSNSI--YPWSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGrETR 244
Cdd:cd01482     2 DIVFLVDGSWSIgrSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG-NTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  245 TAQAIMVACTEGFSESRGGRPEAARLLVVVTDGESHDGEELPaALKACEAGrVTRYGIAVLGHylrrqrDPSsflrEIRA 324
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDDVELP-ARVLRNLG-VNVFAVGVKDA------DES----ELKM 148

                         170
                  ....*....|....*
gi 164565428  325 IASDPDERFFFNVTD 339
Cdd:cd01482   149 IASKPSETHVFNVAD 163
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 167-339 6.86e-30

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: 116.56  E-value: 6.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  167 DVVIVLDGSNSI--YPWSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRReGRETR 244
Cdd:cd01472     2 DIVFLVDGSESIglSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYI-GGGTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  245 TAQAIMVACTEGFSESRGGRPEAARLLVVVTDGESHDGEELPAalkACEAgrvtRYGIAVLGHYLRRQrDPSsflrEIRA 324
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPA---VELK----QAGIEVFAVGVKNA-DEE----ELKQ 148

                         170
                  ....*....|....*
gi 164565428  325 IASDPDERFFFNVTD 339
Cdd:cd01472   149 IASDPKELYVFNVAD 163
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 167-335 1.17e-23

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: 98.79  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  167 DVVIVLDGSNSI--YPWSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGRETR 244
Cdd:cd00198     2 DIVFLLDVSGSMggEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  245 TAQAIMVACTEGFSESRGGRPeaaRLLVVVTDGESHDGEELPA-ALKACEAGRVTRYGIAVLGHYLRRQrdpssflreIR 323
Cdd:cd00198    82 IGAALRLALELLKSAKRPNAR---RVIILLTDGEPNDGPELLAeAARELRKLGITVYTIGIGDDANEDE---------LK 149

                         170
                  ....*....|..
gi 164565428  324 AIASDPDERFFF 335
Cdd:cd00198   150 EIADKTTGGAVF 161
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 167-339 3.61e-22

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: 96.30  E-value: 3.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  167 DVVIVLDGSNSIYP--WSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREgRETR 244
Cdd:cd01475     4 DLVFLIDSSRSVRPenFELVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLE-TGTM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  245 TAQAIMVACTEGFSESRGGRPEAA---RLLVVVTDGESHDGEELPAAlKACEAGrVTRYGIAVlghylrrqrdPSSFLRE 321
Cdd:cd01475    83 TGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAA-KARALG-IEMFAVGV----------GRADEEE 150

                         170
                  ....*....|....*...
gi 164565428  322 IRAIASDPDERFFFNVTD 339
Cdd:cd01475   151 LREIASEPLADHVFYVED 168
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 167-334 7.97e-21

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: 90.54  E-value: 7.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  167 DVVIVLDGSNSIYPWSEVQ-TFLRRLVGRLFIDPEQIQVGLVQY-GENPVH-EWSLGDFRTKEEVVRAARNLSRREGrET 243
Cdd:cd01476     2 DLLFVLDSSGSVRGKFEKYkKYIERIVEGLEIGPTATRVALITYsGRGRQRvRFNLPKHNDGEELLEKVDNLRFIGG-TT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  244 RTAQAIMVAcTEGFSESRGGRPEAARLLVVVTDGESHDGEElpaalkacEAGRVTR-----YGIAVLGHylrrqrDPSSF 318
Cdd:cd01476    81 ATGAAIEVA-LQQLDPSEGRREGIPKVVVVLTDGRSHDDPE--------KQARILRavpniETFAVGTG------DPGTV 145

                         170
                  ....*....|....*..
gi 164565428  319 L-REIRAIASDPDERFF 334
Cdd:cd01476   146 DtEELHSITGNEDHIFT 162
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 167-339 7.19e-20

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: 87.76  E-value: 7.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  167 DVVIVLDGSNSIYP--WSEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAARNLSRREGRETR 244
Cdd:cd01481     2 DIVFLIDGSDNVGSgnFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  245 TAQAIMVACTEGFSESRGGRPEAA--RLLVVVTDGESHDGEELPaalkaceAGRVTRYGIAVLGhYLRRQRDPSsflrEI 322
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRIEEGvpQFLVLITGGKSQDDVERP-------AVALKRAGIVPFA-IGARNADLA----EL 149

                         170
                  ....*....|....*..
gi 164565428  323 RAIASDPDerFFFNVTD 339
Cdd:cd01481   150 QQIAFDPS--FVFQVSD 164
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 166-306 6.47e-15

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: 74.34  E-value: 6.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  166 MDVVIVLDGSNSI--YPW-SEVQTFLRRLVGRLFIDPEQIQVGLVQYGENPVHEWSLGDFRTKEE-----VVRAARNLSR 237
Cdd:cd01471     1 LDLYLLVDGSGSIgySNWvTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLYY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164565428  238 REGReTRTAQAIMVaCTEGFSESRGGRPEAARLLVVVTDGESHDgeeLPAALKACEAGRVTRYGIAVLG 306
Cdd:cd01471    81 PNGS-TNTTSALLV-VEKHLFDTRGNRENAPQLVIIMTDGIPDS---KFRTLKEARKLRERGVIIAVLG 144
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 545-599 2.03e-12

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: 62.78  E-value: 2.03e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 164565428    545 QDSRFGFAMAALPDLNHDGFSDVAVGAPLED--GHQGALYLYHGTQTGIRPHPTQRI 599
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANdaGETGAVYVYFGSSGGGNSIPLQNL 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 145-351 1.03e-08

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 57.64  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  145 VDASFRLQGSLAPTAQRCPTYMDVVIVLDGSNSIY---PWSEVQTFLRRLVGRLfidPEQIQVGLVQYGENPvhEWSLGD 221
Cdd:COG1240    72 VLLLLLALALAPLALARPQRGRDVVLVVDASGSMAaenRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEA--EVLLPL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  222 FRTKEEVVRAARNLSRREGreTRTAQAIMVACTEGfsesRGGRPEAARLLVVVTDGESHDG-EELPAALKACEAGRVTRY 300
Cdd:COG1240   147 TRDREALKRALDELPPGGG--TPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGrIDPLEAAELAAAAGIRIY 220

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 164565428  301 GIAVLGHYLRRQrdpssFLREIrAIASDPDerfFFNVTDEAALTDIVDALG 351
Cdd:COG1240   221 TIGVGTEAVDEG-----LLREI-AEATGGR---YFRADDLSELAAIYREID 262
VWA_2 pfam13519
von Willebrand factor type A domain;
168-274 5.51e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 51.91  E-value: 5.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428   168 VVIVLDGSNSIYP-------WSEVQTFLRRLVGRLfidPEQiQVGLVQYGENPVHEWSLGDfrTKEEVVRAARNLSRREG 240
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygptrLEAAKDAVLALLKSL---PGD-RVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 164565428   241 rETRTAQAIMVActegFSESRGGRPEAARLLVVV 274
Cdd:pfam13519   75 -GTNLAAALQLA----RAALKHRRKNQPRRIVLI 103
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 549-584 1.25e-06

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: 45.96  E-value: 1.25e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 164565428   549 FGFAMAALpDLNHDGFSDVAVGAPLEDG-HQGALYLY 584
Cdd:pfam01839    1 FGYSVAVG-DLNGDGYADLAVGAPGEGGaGAGAVYVL 36
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 162-312 1.93e-05

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: 46.61  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  162 CPtyMDVVIVLDGSNSI--YPWSEVQTFLRRLVGRLF------IDPEQIQVGLVQYGENPVHEWSLGDFRTKEEVVRAAR 233
Cdd:cd01480     1 GP--VDITFVLDSSESVglQNFDITKNFVKRVAERFLkdyyrkDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164565428  234 NLSRREGRETRTAQAIMVACTEGFSESRGGRpeaARLLVVVTDGEShDGEELPAALKA-CEAGRVtryGIAVLGHYLRRQ 312
Cdd:cd01480    79 DNLEYIGGGTFTDCALKYATEQLLEGSHQKE---NKFLLVITDGHS-DGSPDGGIEKAvNEADHL---GIKIFFVAVGSQ 151
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 482-525 1.39e-04

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 40.82  E-value: 1.39e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 164565428    482 IGSYFGSELCPL-DTDMDGITNiLLVAAPMflGPQNKETGRIYVY 525
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPD-LLVGAPR--ANDAGETGAVYVY 42
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 41-81 5.17e-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: 36.20  E-value: 5.17e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 164565428     41 FGYSVLQHV---GGGQRWMLVGAPWDGPSGdRKGDVYRCSIGGF 81
Cdd:smart00191    5 FGYSVAGVGdvnGDGYPDLLVGAPRANDAG-ETGAVYVYFGSSG 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.
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