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Conserved domains on  [gi|109077202|ref|XP_001094788|]
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integrin alpha-1 [Macaca mulatta]

Protein Classification

integrin alpha( domain architecture ID 11546366)

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

CATH:  2.130.10.130|2.60.40.1460|2.60.40.1510|2.60.40.1530|3.40.50.410
Gene Ontology:  GO:0007155|GO:0008305|GO:0005178|GO:0046872
PubMed:  3028640|2199285|12297042|12826403|14689578|12361595|12234368

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 ...
 171-351 2.03e-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: 280.01  E-value: 2.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSIYP--WDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRqT 248
Cdd:cd01469     1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  249 MTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRgnlstEKFVEEIK 328
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQR-----ENSREELK 154

                         170       180
                  ....*....|....*....|...
gi 109077202  329 SIASEPTEKHFFNVSDELALVTI 351
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 ...
 665-1033 6.75e-55

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: 198.31  E-value: 6.75e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   665 RDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSK-EDTIyeaDLQYRVTLDSLRQ---ISRSFFSGT 740
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFSYTGKPIpNPSL---VLNYELELDRQKKkglPPRVLFLDS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   741 QERKVQRNITVRKS---ECTKHSFYMLDkhDFQD---SVRITLDFNLTDPENG--------PVLDDSLPNSVHEYIPFAK 806
Cdd:pfam08441   78 QQPSLTGTLVLLSQgrkVCRTTKAYLRD--EFRDklsPIVISLNYSLRVDPRApsdlpglkPILDQNQPSTVQEQANFLK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   807 DCGNKEKCISDLSLHVA---TTEKDLLIVRSQNDkFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKD---SCES 880
Cdd:pfam08441  156 DCGEDNVCVPDLQLSAKfdsRESDEPLLLGDDND-LALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEkqlSCTA 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   881 NHNIT-----CKVGYPFLRkGEMVTFKILfqFNTSYLMEN---VTIYLNATSDSEEPPEtlsDNVVNISIPVKYEVGLQF 952
Cdd:pfam08441  235 KKENStrqvvCDLGNPMKR-GTQVTFGLR--FSVSGLELSteeLSFDLQIRSTNEQNSN---SNPVSLKVPVVAEAQLSL 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   953 Y--SSASEYHISIAANETvPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSDNANC 1030
Cdd:pfam08441  309 SgvSKPDQVVGGSVKGES-AMKPRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGKWLLYLLDVQGQGKGEC 387


                   ...
gi 109077202  1031 RPH 1033
Cdd:pfam08441  388 SPQ 390
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 568-621 1.65e-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: 66.24  E-value: 1.65e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 109077202    568 GARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHG--GAVYIYHGSGKTIRKEYAQRI 621
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 486-529 1.38e-07

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 49.30  E-value: 1.38e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 109077202    486 IGSYFG-SILTTIDIDKDSNTDiLLVGAPMYMGTekEEQGKVYVY 529
Cdd:smart00191    1 PGSYFGySVAGVGDVNGDGYPD-LLVGAPRANDA--GETGAVYVY 42
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 434-474 7.16e-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: 35.81  E-value: 7.16e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 109077202    434 SYLGYTVNSATASSGD--VLYIAGQPRYNH---TGQVIIYRMEDGN 474
Cdd:smart00191    3 SYFGYSVAGVGDVNGDgyPDLLVGAPRANDageTGAVYVYFGSSGG 48
 
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 ...
 171-351 2.03e-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: 280.01  E-value: 2.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSIYP--WDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRqT 248
Cdd:cd01469     1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  249 MTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRgnlstEKFVEEIK 328
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQR-----ENSREELK 154

                         170       180
                  ....*....|....*....|...
gi 109077202  329 SIASEPTEKHFFNVSDELALVTI 351
Cdd:cd01469   155 TIASKPPEEHFFNVTDFAALKDI 177
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 665-1033 6.75e-55

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: 198.31  E-value: 6.75e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   665 RDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSK-EDTIyeaDLQYRVTLDSLRQ---ISRSFFSGT 740
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFSYTGKPIpNPSL---VLNYELELDRQKKkglPPRVLFLDS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   741 QERKVQRNITVRKS---ECTKHSFYMLDkhDFQD---SVRITLDFNLTDPENG--------PVLDDSLPNSVHEYIPFAK 806
Cdd:pfam08441   78 QQPSLTGTLVLLSQgrkVCRTTKAYLRD--EFRDklsPIVISLNYSLRVDPRApsdlpglkPILDQNQPSTVQEQANFLK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   807 DCGNKEKCISDLSLHVA---TTEKDLLIVRSQNDkFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKD---SCES 880
Cdd:pfam08441  156 DCGEDNVCVPDLQLSAKfdsRESDEPLLLGDDND-LALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEkqlSCTA 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   881 NHNIT-----CKVGYPFLRkGEMVTFKILfqFNTSYLMEN---VTIYLNATSDSEEPPEtlsDNVVNISIPVKYEVGLQF 952
Cdd:pfam08441  235 KKENStrqvvCDLGNPMKR-GTQVTFGLR--FSVSGLELSteeLSFDLQIRSTNEQNSN---SNPVSLKVPVVAEAQLSL 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   953 Y--SSASEYHISIAANETvPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSDNANC 1030
Cdd:pfam08441  309 SgvSKPDQVVGGSVKGES-AMKPRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGKWLLYLLDVQGQGKGEC 387


                   ...
gi 109077202  1031 RPH 1033
Cdd:pfam08441  388 SPQ 390
VWA pfam00092
von Willebrand factor type A domain;
172-353 2.53e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 178.24  E-value: 2.53e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   172 DIVIVLDGSNSI--YPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTM 249
Cdd:pfam00092    1 DIVFLLDGSGSIggDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   250 TALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNhRLKKVIQDCEDENIQRFSIAILGSYNrgnlstekfvEEIKS 329
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG-DPEEVARELKSAGVTVFAVGVGNADD----------EELRK 149

                          170       180
                   ....*....|....*....|....
gi 109077202   330 IASEPTEKHFFNVSDELALVTIVK 353
Cdd:pfam00092  150 IASEPGEGHVFTVSDFEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 172-352 1.44e-44

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: 159.16  E-value: 1.44e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202    172 DIVIVLDGSNSIYP--WDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTM 249
Cdd:smart00327    1 DVVFLLDGSGSMGGnrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202    250 TALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDN-HRLKKVIQDCEDENIQRFSIAILGSYNRgnlstekfvEEIK 328
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpKDLLKAAKELKRSGVKVFVVGVGNDVDE---------EELK 151

                           170       180
                    ....*....|....*....|....
gi 109077202    329 SIASEPTEKHFFNVSDELALVTIV 352
Cdd:smart00327  152 KLASAPGGVYVFLPELLDLLIDLL 175
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 568-621 1.65e-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: 66.24  E-value: 1.65e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 109077202    568 GARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHG--GAVYIYHGSGKTIRKEYAQRI 621
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGGNSIPLQNL 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 171-356 1.65e-09

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: 59.95  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSIY---PWDSVTAFLNDLLERMdigPKQTQVGIVQYGENVTHEFNLNkySSTEEVLVAAKKIVQRGGrq 247
Cdd:COG1240    93 RDVVLVVDASGSMAaenRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGG-- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  248 tmTAL--GIDTARKEAfteaRGARRGVKKVMVIVTDGESHD-NHRLKKVIQDCEDENIQRFSIAI-LGSYNRGNLstekf 323
Cdd:COG1240   166 --TPLgdALALALELL----KRADPARRKVIVLLTDGRDNAgRIDPLEAAELAAAAGIRIYTIGVgTEAVDEGLL----- 234

                         170       180       190
                  ....*....|....*....|....*....|...
gi 109077202  324 veeiKSIASEpTEKHFFNVSDELALVTIVKTLG 356
Cdd:COG1240   235 ----REIAEA-TGGRYFRADDLSELAAIYREID 262
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 571-606 3.64e-08

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 50.20  E-value: 3.64e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 109077202   571 FGTAIAAVkDLNLDGFNDIVIGAPLEDDHG-GAVYIY 606
Cdd:pfam01839    1 FGYSVAVG-DLNGDGYADLAVGAPGEGGAGaGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 486-529 1.38e-07

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 49.30  E-value: 1.38e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 109077202    486 IGSYFG-SILTTIDIDKDSNTDiLLVGAPMYMGTekEEQGKVYVY 529
Cdd:smart00191    1 PGSYFGySVAGVGDVNGDGYPD-LLVGAPRANDA--GETGAVYVY 42
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 490-529 3.65e-05

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 41.73  E-value: 3.65e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 109077202   490 FGSILTTIDIDKDSNTDiLLVGAPMYMGTekeEQGKVYVY 529
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAPGEGGA---GAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 434-474 7.16e-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: 35.81  E-value: 7.16e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 109077202    434 SYLGYTVNSATASSGD--VLYIAGQPRYNH---TGQVIIYRMEDGN 474
Cdd:smart00191    3 SYFGYSVAGVGDVNGDgyPDLLVGAPRANDageTGAVYVYFGSSGG 48
 
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 ...
 171-351 2.03e-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: 280.01  E-value: 2.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSIYP--WDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRqT 248
Cdd:cd01469     1 MDIVFVLDGSGSIYPddFQKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGL-T 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  249 MTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRgnlstEKFVEEIK 328
Cdd:cd01469    80 NTATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLLKDVIPQAEREGIIRYAIGVGGHFQR-----ENSREELK 154

                         170       180
                  ....*....|....*....|...
gi 109077202  329 SIASEPTEKHFFNVSDELALVTI 351
Cdd:cd01469   155 TIASKPPEEHFFNVTDFAALKDI 177
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 665-1033 6.75e-55

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: 198.31  E-value: 6.75e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   665 RDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSK-EDTIyeaDLQYRVTLDSLRQ---ISRSFFSGT 740
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVSCFTVRACFSYTGKPIpNPSL---VLNYELELDRQKKkglPPRVLFLDS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   741 QERKVQRNITVRKS---ECTKHSFYMLDkhDFQD---SVRITLDFNLTDPENG--------PVLDDSLPNSVHEYIPFAK 806
Cdd:pfam08441   78 QQPSLTGTLVLLSQgrkVCRTTKAYLRD--EFRDklsPIVISLNYSLRVDPRApsdlpglkPILDQNQPSTVQEQANFLK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   807 DCGNKEKCISDLSLHVA---TTEKDLLIVRSQNDkFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKD---SCES 880
Cdd:pfam08441  156 DCGEDNVCVPDLQLSAKfdsRESDEPLLLGDDND-LALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEkqlSCTA 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   881 NHNIT-----CKVGYPFLRkGEMVTFKILfqFNTSYLMEN---VTIYLNATSDSEEPPEtlsDNVVNISIPVKYEVGLQF 952
Cdd:pfam08441  235 KKENStrqvvCDLGNPMKR-GTQVTFGLR--FSVSGLELSteeLSFDLQIRSTNEQNSN---SNPVSLKVPVVAEAQLSL 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   953 Y--SSASEYHISIAANETvPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSDNANC 1030
Cdd:pfam08441  309 SgvSKPDQVVGGSVKGES-AMKPRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGKWLLYLLDVQGQGKGEC 387


                   ...
gi 109077202  1031 RPH 1033
Cdd:pfam08441  388 SPQ 390
VWA pfam00092
von Willebrand factor type A domain;
172-353 2.53e-51

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 178.24  E-value: 2.53e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   172 DIVIVLDGSNSI--YPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTM 249
Cdd:pfam00092    1 DIVFLLDGSGSIggDNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   250 TALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNhRLKKVIQDCEDENIQRFSIAILGSYNrgnlstekfvEEIKS 329
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG-DPEEVARELKSAGVTVFAVGVGNADD----------EELRK 149

                          170       180
                   ....*....|....*....|....
gi 109077202   330 IASEPTEKHFFNVSDELALVTIVK 353
Cdd:pfam00092  150 IASEPGEGHVFTVSDFEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 172-352 1.44e-44

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: 159.16  E-value: 1.44e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202    172 DIVIVLDGSNSIYP--WDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTM 249
Cdd:smart00327    1 DVVFLLDGSGSMGGnrFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202    250 TALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDN-HRLKKVIQDCEDENIQRFSIAILGSYNRgnlstekfvEEIK 328
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGpKDLLKAAKELKRSGVKVFVVGVGNDVDE---------EELK 151

                           170       180
                    ....*....|....*....|....
gi 109077202    329 SIASEPTEKHFFNVSDELALVTIV 352
Cdd:smart00327  152 KLASAPGGVYVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 171-340 2.19e-39

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: 143.59  E-value: 2.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSIYP--WDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQT 248
Cdd:cd01450     1 LDIVFLLDGSESVGPenFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  249 MTALGIDTARKEAFTEaRGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAIlGSYNRgnlstekfvEEIK 328
Cdd:cd01450    81 NTGKALQYALEQLFSE-SNARENVPKVIIVLTDGRSDDGGDPKEAAAKLKDEGIKVFVVGV-GPADE---------EELR 149

                         170
                  ....*....|..
gi 109077202  329 SIASEPTEKHFF 340
Cdd:cd01450   150 EIASCPSERHVF 161
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 172-344 4.90e-35

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: 131.20  E-value: 4.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  172 DIVIVLDGSNSI--YPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGrQTM 249
Cdd:cd01472     2 DIVFLVDGSESIglSNFNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGG-GTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  250 TALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKViqdcedeNIQRFSIAILGSYNRGNLStekfvEEIKS 329
Cdd:cd01472    81 TGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAV-------ELKQAGIEVFAVGVKNADE-----EELKQ 148

                         170
                  ....*....|....*
gi 109077202  330 IASEPTEKHFFNVSD 344
Cdd:cd01472   149 IASDPKELYVFNVAD 163
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 172-344 1.72e-34

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: 129.71  E-value: 1.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  172 DIVIVLDGSNSI--YPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGrQTM 249
Cdd:cd01482     2 DIVFLVDGSWSIgrSNFNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGG-NTR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  250 TALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNhrLKKVIQDCEDENIQRFSIAIlgsynrgnlsTEKFVEEIKS 329
Cdd:cd01482    81 TGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQDD--VELPARVLRNLGVNVFAVGV----------KDADESELKM 148

                         170
                  ....*....|....*
gi 109077202  330 IASEPTEKHFFNVSD 344
Cdd:cd01482   149 IASKPSETHVFNVAD 163
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 171-359 7.44e-32

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: 124.42  E-value: 7.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSIYPWD--SVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRgGRQT 248
Cdd:cd01475     3 TDLVFLIDSSRSVRPENfeLVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYL-ETGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  249 MTALGIDTARKEAFTEARGARRG---VKKVMVIVTDGESHDNhrLKKVIQDCEDENIQRFSIAIlgsynrGNLStekfVE 325
Cdd:cd01475    82 MTGLAIQYAMNNAFSEAEGARPGserVPRVGIVVTDGRPQDD--VSEVAAKARALGIEMFAVGV------GRAD----EE 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 109077202  326 EIKSIASEPTEKHFFNVSDELALVTIVKTLGERI 359
Cdd:cd01475   150 ELREIASEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 171-340 3.13e-29

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: 114.59  E-value: 3.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSI--YPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQT 248
Cdd:cd00198     1 ADIVFLLDVSGSMggEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  249 MTALGIDTARKEAFTEARGARRgvkKVMVIVTDGESHDNHR-LKKVIQDCEDENIQRFSIAILGSYNRgnlstekfvEEI 327
Cdd:cd00198    81 NIGAALRLALELLKSAKRPNAR---RVIILLTDGEPNDGPElLAEAARELRKLGITVYTIGIGDDANE---------DEL 148

                         170
                  ....*....|...
gi 109077202  328 KSIASEPTEKHFF 340
Cdd:cd00198   149 KEIADKTTGGAVF 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 172-344 1.10e-22

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: 95.85  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  172 DIVIVLDGSNSIYP--WDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTM 249
Cdd:cd01481     2 DIVFLIDGSDNVGSgnFPAIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRLRLRGGSQLN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  250 TALGIDTARKEAFTEARGAR--RGVKKVMVIVTDGESHDNHRLKKVIqdcedenIQRFSIAILGSynrGNLSTEKfvEEI 327
Cdd:cd01481    82 TGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVA-------LKRAGIVPFAI---GARNADL--AEL 149

                         170
                  ....*....|....*..
gi 109077202  328 KSIASEPteKHFFNVSD 344
Cdd:cd01481   150 QQIAFDP--SFVFQVSD 164
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 171-287 8.00e-18

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: 82.06  E-value: 8.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSIYP-WDSVTAFLNDLLERMDIGPKQTQVGIVQY-GENVTH-EFNLNKYSSTEEVLVAAKKIVQRGGrQ 247
Cdd:cd01476     1 LDLLFVLDSSGSVRGkFEKYKKYIERIVEGLEIGPTATRVALITYsGRGRQRvRFNLPKHNDGEELLEKVDNLRFIGG-T 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 109077202  248 TMTALGIDTARKEaFTEARGARRGVKKVMVIVTDGESHDN 287
Cdd:cd01476    80 TATGAAIEVALQQ-LDPSEGRREGIPKVVVVLTDGRSHDD 118
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 568-621 1.65e-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: 66.24  E-value: 1.65e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 109077202    568 GARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHG--GAVYIYHGSGKTIRKEYAQRI 621
Cdd:smart00191    2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGGNSIPLQNL 57
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 171-315 4.45e-13

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: 68.95  E-value: 4.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSI--YPW-DSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEE-----VLVAAKKIVQ 242
Cdd:cd01471     1 LDLYLLVDGSGSIgySNWvTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKdlalnAIRALLSLYY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  243 RGGRqTMTALGIDTARKEAFtEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQrfsIAILG-------SYNR 315
Cdd:cd01471    81 PNGS-TNTTSALLVVEKHLF-DTRGNRENAPQLVIIMTDGIPDSKFRTLKEARKLRERGVI---IAVLGvgqgvnhEENR 155
VWA_2 pfam13519
von Willebrand factor type A domain;
173-279 5.77e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 60.38  E-value: 5.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202   173 IVIVLDGSNSIYP-------WDSVTAFLNDLLERMDIgpkqTQVGIVQYGENVTHEFNLNKysSTEEVLVAAKKIVQRGG 245
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygptrLEAAKDAVLALLKSLPG----DRVGLVTFGDGPEVLIPLTK--DRAKILRALRRLEPKGG 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 109077202   246 rQTMTALGIDTARKEAFTEargaRRGVKKVMVIV 279
Cdd:pfam13519   75 -GTNLAAALQLARAALKHR----RKNQPRRIVLI 103
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 171-319 1.32e-09

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 58.94  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSI--YPWDSVTAFLNDLLERM------DIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQ 242
Cdd:cd01480     3 VDITFVLDSSESVglQNFDITKNFVKRVAERFlkdyyrKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  243 RGGRQTMTalgiDTARKEAFTEARGARR-GVKKVMVIVTDGESH--DNHRLKKVIQDCEDENIQRFSIAIlGSYNRGNLS 319
Cdd:cd01480    83 YIGGGTFT----DCALKYATEQLLEGSHqKENKFLLVITDGHSDgsPDGGIEKAVNEADHLGIKIFFVAV-GSQNEEPLS 157
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 171-356 1.65e-09

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: 59.95  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  171 LDIVIVLDGSNSIY---PWDSVTAFLNDLLERMdigPKQTQVGIVQYGENVTHEFNLNkySSTEEVLVAAKKIVQRGGrq 247
Cdd:COG1240    93 RDVVLVVDASGSMAaenRLEAAKGALLDFLDDY---RPRDRVGLVAFGGEAEVLLPLT--RDREALKRALDELPPGGG-- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  248 tmTAL--GIDTARKEAfteaRGARRGVKKVMVIVTDGESHD-NHRLKKVIQDCEDENIQRFSIAI-LGSYNRGNLstekf 323
Cdd:COG1240   166 --TPLgdALALALELL----KRADPARRKVIVLLTDGRDNAgRIDPLEAAELAAAAGIRIYTIGVgTEAVDEGLL----- 234

                         170       180       190
                  ....*....|....*....|....*....|...
gi 109077202  324 veeiKSIASEpTEKHFFNVSDELALVTIVKTLG 356
Cdd:COG1240   235 ----REIAEA-TGGRYFRADDLSELAAIYREID 262
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 571-606 3.64e-08

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 50.20  E-value: 3.64e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 109077202   571 FGTAIAAVkDLNLDGFNDIVIGAPLEDDHG-GAVYIY 606
Cdd:pfam01839    1 FGYSVAVG-DLNGDGYADLAVGAPGEGGAGaGAVYVL 36
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 167-287 6.61e-08

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: 54.05  E-value: 6.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  167 CSTQLDIVIVLDGSNSI-YPWDSVTAFLNDLLERMdIGPkQTQVGIVQYGENVTHEFNLNKYSSTE-EVLVAAKKIVQRG 244
Cdd:cd01474     1 CAGHFDLYFVLDKSGSVaANWIEIYDFVEQLVDRF-NSP-GLRFSFITFSTRATKILPLTDDSSAIiKGLEVLKKVTPSG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 109077202  245 grQTMTALGIDTARKEAFTEARGARRgVKKVMVIVTDGESHDN 287
Cdd:cd01474    79 --QTYIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLN 118
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 486-529 1.38e-07

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 49.30  E-value: 1.38e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 109077202    486 IGSYFG-SILTTIDIDKDSNTDiLLVGAPMYMGTekEEQGKVYVY 529
Cdd:smart00191    1 PGSYFGySVAGVGDVNGDGYPD-LLVGAPRANDA--GETGAVYVY 42
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 580-651 8.50e-06

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: 44.14  E-value: 8.50e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109077202   580 DLNLDGFNDIVIGapleDDHGGAVYIYHGSGkTIRKEYAQRIPSGGDGETLKFFgqsihgemDLNGDGLTDV 651
Cdd:pfam13517    1 DLDGDGKLDLVVA----NDGGLRLYLNNGDG-TFTFITSVSLGGGGGGLSVAVG--------DLDGDGRLDL 59
vWA_F09G8-8_type cd01477
VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 165-280 1.21e-05

VWA F09G8.8 type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. The members of this subgroup lack the MIDAS motif. This subgroup is found only in C. elegans and the members identified thus far are always found fused to a C-Lectin type domain. Biochemical function thus far has not be attributed to any of the members of this subgroup.


Pssm-ID: 238754 [Multi-domain]  Cd Length: 193  Bit Score: 47.42  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109077202  165 RECST-----QLDIVIVLDGS-----NSIYpwdSVTAFLNDLLERMDIG------PKQTQVGIVQYGENVTHEFNLNKYS 228
Cdd:cd01477     9 RECGSdiknlWLDIVFVVDNSkgmtqGGLW---QVRATISSLFGSSSQIgtdyddPRSTRVGLVTYNSNATVVADLNDLQ 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 109077202  229 STEEVlvaaKKIVQRG------GRQTMTALGIDTARKEAFTEARGARRGVKKVMVIVT 280
Cdd:cd01477    86 SFDDL----YSQIQGSltdvssTNASYLDTGLQAAEQMLAAGKRTSRENYKKVVIVFA 139
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 490-529 3.65e-05

FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.


Pssm-ID: 460357  Cd Length: 36  Bit Score: 41.73  E-value: 3.65e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 109077202   490 FGSILTTIDIDKDSNTDiLLVGAPMYMGTekeEQGKVYVY 529
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAPGEGGA---GAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 434-474 7.16e-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: 35.81  E-value: 7.16e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 109077202    434 SYLGYTVNSATASSGD--VLYIAGQPRYNH---TGQVIIYRMEDGN 474
Cdd:smart00191    3 SYFGYSVAGVGDVNGDgyPDLLVGAPRANDageTGAVYVYFGSSGG 48
 
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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