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Conserved domains on  [gi|1239906661|ref|XP_022275563|]
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integrin alpha-L isoform X2 [Canis lupus familiaris]

Protein Classification

integrin alpha( domain architecture ID 11619903)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 59-227 1.46e-71

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


The actual alignment was detected with superfamily member cd01469:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 177  Bit Score: 235.33  E-value: 1.46e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   59 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSN--SSYQFAAVQFSTDCKTEFNFLDYVKVKNPDVLLGKVVHMRLLTN 136
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  137 TFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD----RANIDSAK--DIIRYIIGIGKHFATKRSQETLHQFASKP 210
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                          170
                   ....*....|....*..
gi 1239906661  211 AEEFVKILDTFEKLKDL 227
Cdd:cd01469    161 PEEHFFNVTDFAALKDI 177
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 517-902 1.10e-30

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: 126.67  E-value: 1.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  517 RPVVDILTHISFSPAEIPVHEVECSHSTSNKKkeGVNITVCFQVKPLTLqFRGRLVANliYTLQLD---GHRTRSRGLFP 593
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS--CFTVRACFSYTGKPI-PNPSLVLN--YELELDrqkKKGLPPRVLFL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  594 GGRQ-ELSGNIAVTR--DWSCIKLWFHFPVCIQDLISPINVSLNFSLweeEETPRNKRALDrDIRPIL---RPLphVANT 667
Cdd:pfam08441   76 DSQQpSLTGTLVLLSqgRKVCRTTKAYLRDEFRDKLSPIVISLNYSL---RVDPRAPSDLP-GLKPILdqnQPS--TVQE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  668 EIPFEKNCGEDKKCEADLGLSFSP---AGSRVLRLIPSASLSVELILSNLREDAYSVHLNLSFPQGLSFRKVEMLKPHSQ 744
Cdd:pfam08441  150 QANFLKDCGEDNVCVPDLQLSAKFdsrESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  745 IpvSCEelpevAKLMN--RIVSCNVSSPiFRAGSVVAIQVMF---HMLLNsswGDSVELHANVSCHNEDSGLLEnnlatt 819
Cdd:pfam08441  230 L--SCT-----AKKENstRQVVCDLGNP-MKRGTQVTFGLRFsvsGLELS---TEELSFDLQIRSTNEQNSNSN------ 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  820 tiPVLYPINILTEDK------ENSTLYVGFTPKG-PKMYF---------VEHFYQVRIQ-PSiydhKVPALEALIGVPVS 882
Cdd:pfam08441  293 --PVSLKVPVVAEAQlslsgvSKPDQVVGGSVKGeSAMKPrseedigplVEHTYEVINNgPS----TVSGASLEISWPYE 366

                          410       420
                   ....*....|....*....|....*
gi 1239906661  883 HSEGpithKW-----NVEMEPPVTC 902
Cdd:pfam08441  367 LSNG----KWllyllDVQGQGKGEC 387
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 421-473 5.84e-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: 64.32  E-value: 5.84e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1239906661   421 PLGRFGAAITALTDINGDGLVDVAVGAPLE----EKGAVYIFNGQHGGLSPQPSQRI 473
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 360-407 2.44e-08

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 51.22  E-value: 2.44e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1239906661   360 IGSYFGGELCGV-DIDQDGETELLlIGAPLFYGEQRGGRVFIYQRKQLG 407
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 483-528 8.99e-05

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 41.21  E-value: 8.99e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1239906661   483 QWFGRSIHGVKDLGGDGLTDVAVGA--------EGQVIVLSSRPVVDILTHISF 528
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1017-1031 3.02e-03

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


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 35.94  E-value: 3.02e-03
                           10
                   ....*....|....*
gi 1239906661 1017 KLGFFKRNLKEKMEA 1031
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 306-355 8.50e-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: 8.50e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1239906661   306 GYLGYTVTW---LYSRGLTSLLAaGAPRYQH---VGRVVLFQESKDKEHWSQIQKI 355
Cdd:smart00191    3 SYFGYSVAGvgdVNGDGYPDLLV-GAPRANDageTGAVYVYFGSSGGGNSIPLQNL 57
 
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 ...
 59-227 1.46e-71

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: 235.33  E-value: 1.46e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   59 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSN--SSYQFAAVQFSTDCKTEFNFLDYVKVKNPDVLLGKVVHMRLLTN 136
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  137 TFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD----RANIDSAK--DIIRYIIGIGKHFATKRSQETLHQFASKP 210
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                          170
                   ....*....|....*..
gi 1239906661  211 AEEFVKILDTFEKLKDL 227
Cdd:cd01469    161 PEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
60-230 7.45e-41

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 148.19  E-value: 7.45e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   60 DLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSNS--SYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL--- 134
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGpdGTRVGLVQYSSDVRTEFPLNDY---SSKEELLSAVDNLRYLggg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  135 -TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD---RANIDSAKD--IIRYIIGIGKHFAtkrsqETLHQFAS 208
Cdd:pfam00092   78 tTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgdpEEVARELKSagVTVFAVGVGNADD-----EELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 1239906661  209 KPAEEFVKILDTFEKLKDLFTE 230
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 60-224 1.68e-31

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: 121.41  E-value: 1.68e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661    60 DLVFLFDGSMSLQQDEFQKILDFMKDVMKKL--SNSSYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL--- 134
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDS---RSKDALLEALASLSYKlgg 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   135 -TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD-----RANIDSAKD--IIRYIIGIGKHFatkrSQETLHQF 206
Cdd:smart00327   78 gTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkdlLKAAKELKRsgVKVFVVGVGNDV----DEEELKKL 153

                           170
                    ....*....|....*...
gi 1239906661   207 ASKPAEEFVKILDTFEKL 224
Cdd:smart00327  154 ASAPGGVYVFLPELLDLL 171
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 517-902 1.10e-30

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: 126.67  E-value: 1.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  517 RPVVDILTHISFSPAEIPVHEVECSHSTSNKKkeGVNITVCFQVKPLTLqFRGRLVANliYTLQLD---GHRTRSRGLFP 593
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS--CFTVRACFSYTGKPI-PNPSLVLN--YELELDrqkKKGLPPRVLFL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  594 GGRQ-ELSGNIAVTR--DWSCIKLWFHFPVCIQDLISPINVSLNFSLweeEETPRNKRALDrDIRPIL---RPLphVANT 667
Cdd:pfam08441   76 DSQQpSLTGTLVLLSqgRKVCRTTKAYLRDEFRDKLSPIVISLNYSL---RVDPRAPSDLP-GLKPILdqnQPS--TVQE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  668 EIPFEKNCGEDKKCEADLGLSFSP---AGSRVLRLIPSASLSVELILSNLREDAYSVHLNLSFPQGLSFRKVEMLKPHSQ 744
Cdd:pfam08441  150 QANFLKDCGEDNVCVPDLQLSAKFdsrESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  745 IpvSCEelpevAKLMN--RIVSCNVSSPiFRAGSVVAIQVMF---HMLLNsswGDSVELHANVSCHNEDSGLLEnnlatt 819
Cdd:pfam08441  230 L--SCT-----AKKENstRQVVCDLGNP-MKRGTQVTFGLRFsvsGLELS---TEELSFDLQIRSTNEQNSNSN------ 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  820 tiPVLYPINILTEDK------ENSTLYVGFTPKG-PKMYF---------VEHFYQVRIQ-PSiydhKVPALEALIGVPVS 882
Cdd:pfam08441  293 --PVSLKVPVVAEAQlslsgvSKPDQVVGGSVKGeSAMKPrseedigplVEHTYEVINNgPS----TVSGASLEISWPYE 366

                          410       420
                   ....*....|....*....|....*
gi 1239906661  883 HSEGpithKW-----NVEMEPPVTC 902
Cdd:pfam08441  367 LSNG----KWllyllDVQGQGKGEC 387
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 421-473 5.84e-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: 64.32  E-value: 5.84e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1239906661   421 PLGRFGAAITALTDINGDGLVDVAVGAPLE----EKGAVYIFNGQHGGLSPQPSQRI 473
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 360-407 2.44e-08

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 51.22  E-value: 2.44e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1239906661   360 IGSYFGGELCGV-DIDQDGETELLlIGAPLFYGEQRGGRVFIYQRKQLG 407
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 425-458 3.06e-07

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 47.51  E-value: 3.06e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1239906661  425 FGAAItALTDINGDGLVDVAVGAPLE---EKGAVYIF 458
Cdd:pfam01839    1 FGYSV-AVGDLNGDGYADLAVGAPGEggaGAGAVYVL 36
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 61-207 5.96e-05

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 46.15  E-value: 5.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   61 LVFLFD--GSMSLQQDEFQK-ILDFMKDVMKKlsnsSYQFAAVQFST----------DCKTEFNFLDYVKVKNPDVLLGK 127
Cdd:TIGR03436   56 VGLVIDtsGSMRNDLDRARAaAIRFLKTVLRP----NDRVFVVTFNTrlrllqdftsDPRLLEAALNRLKPPLRTDYNSS 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  128 VVHMRLL--TNTFGAINYVAREVFRQDLGARPDaTKVLIIITDG----------EATDRANidsAKDIIRYIIGIGKHF- 194
Cdd:TIGR03436  132 GAFVRDGggTALYDAITLAALEQLANALAGIPG-RKALIVISDGgdnrsrdtleRAIDAAQ---RADVAIYSIDARGLRa 207

                          170       180
                   ....*....|....*....|.
gi 1239906661  195 --------ATKRSQETLHQFA 207
Cdd:TIGR03436  208 pdlgagakAGLGGPEALERLA 228
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 483-528 8.99e-05

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 41.21  E-value: 8.99e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1239906661   483 QWFGRSIHGVKDLGGDGLTDVAVGA--------EGQVIVLSSRPVVDILTHISF 528
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 364-401 4.49e-04

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 38.65  E-value: 4.49e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1239906661  364 FGGELCGVDIDQDGETElLLIGAPlFYGEQRGGRVFIY 401
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAP-GEGGAGAGAVYVL 36
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1017-1031 3.02e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 35.94  E-value: 3.02e-03
                           10
                   ....*....|....*
gi 1239906661 1017 KLGFFKRNLKEKMEA 1031
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 306-355 8.50e-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: 8.50e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1239906661   306 GYLGYTVTW---LYSRGLTSLLAaGAPRYQH---VGRVVLFQESKDKEHWSQIQKI 355
Cdd:smart00191    3 SYFGYSVAGvgdVNGDGYPDLLV-GAPRANDageTGAVYVYFGSSGGGNSIPLQNL 57
 
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 ...
 59-227 1.46e-71

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: 235.33  E-value: 1.46e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   59 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSN--SSYQFAAVQFSTDCKTEFNFLDYVKVKNPDVLLGKVVHMRLLTN 136
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  137 TFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD----RANIDSAK--DIIRYIIGIGKHFATKRSQETLHQFASKP 210
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                          170
                   ....*....|....*..
gi 1239906661  211 AEEFVKILDTFEKLKDL 227
Cdd:cd01469    161 PEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
60-230 7.45e-41

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 148.19  E-value: 7.45e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   60 DLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSNS--SYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL--- 134
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGpdGTRVGLVQYSSDVRTEFPLNDY---SSKEELLSAVDNLRYLggg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  135 -TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD---RANIDSAKD--IIRYIIGIGKHFAtkrsqETLHQFAS 208
Cdd:pfam00092   78 tTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgdpEEVARELKSagVTVFAVGVGNADD-----EELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 1239906661  209 KPAEEFVKILDTFEKLKDLFTE 230
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 60-224 1.68e-31

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: 121.41  E-value: 1.68e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661    60 DLVFLFDGSMSLQQDEFQKILDFMKDVMKKL--SNSSYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL--- 134
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDS---RSKDALLEALASLSYKlgg 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   135 -TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD-----RANIDSAKD--IIRYIIGIGKHFatkrSQETLHQF 206
Cdd:smart00327   78 gTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkdlLKAAKELKRsgVKVFVVGVGNDV----DEEELKKL 153

                           170
                    ....*....|....*...
gi 1239906661   207 ASKPAEEFVKILDTFEKL 224
Cdd:smart00327  154 ASAPGGVYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 59-215 2.71e-31

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: 120.47  E-value: 2.71e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   59 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSNS--SYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL-- 134
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGpdKTRVGLVQYSDDVRVEFSLNDY---KSKDDLLKAVKNLKYLgg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  135 --TNTFGAINYVAREVFRQDlGARPDATKVLIIITDGEATDRANIDSAKDIIR------YIIGIGKHfatkrSQETLHQF 206
Cdd:cd01450     78 ggTNTGKALQYALEQLFSES-NARENVPKVIIVLTDGRSDDGGDPKEAAAKLKdegikvFVVGVGPA-----DEEELREI 151


                   ....*....
gi 1239906661  207 ASKPAEEFV 215
Cdd:cd01450    152 ASCPSERHV 160
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 517-902 1.10e-30

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: 126.67  E-value: 1.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  517 RPVVDILTHISFSPAEIPVHEVECSHSTSNKKkeGVNITVCFQVKPLTLqFRGRLVANliYTLQLD---GHRTRSRGLFP 593
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS--CFTVRACFSYTGKPI-PNPSLVLN--YELELDrqkKKGLPPRVLFL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  594 GGRQ-ELSGNIAVTR--DWSCIKLWFHFPVCIQDLISPINVSLNFSLweeEETPRNKRALDrDIRPIL---RPLphVANT 667
Cdd:pfam08441   76 DSQQpSLTGTLVLLSqgRKVCRTTKAYLRDEFRDKLSPIVISLNYSL---RVDPRAPSDLP-GLKPILdqnQPS--TVQE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  668 EIPFEKNCGEDKKCEADLGLSFSP---AGSRVLRLIPSASLSVELILSNLREDAYSVHLNLSFPQGLSFRKVEMLKPHSQ 744
Cdd:pfam08441  150 QANFLKDCGEDNVCVPDLQLSAKFdsrESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  745 IpvSCEelpevAKLMN--RIVSCNVSSPiFRAGSVVAIQVMF---HMLLNsswGDSVELHANVSCHNEDSGLLEnnlatt 819
Cdd:pfam08441  230 L--SCT-----AKKENstRQVVCDLGNP-MKRGTQVTFGLRFsvsGLELS---TEELSFDLQIRSTNEQNSNSN------ 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  820 tiPVLYPINILTEDK------ENSTLYVGFTPKG-PKMYF---------VEHFYQVRIQ-PSiydhKVPALEALIGVPVS 882
Cdd:pfam08441  293 --PVSLKVPVVAEAQlslsgvSKPDQVVGGSVKGeSAMKPrseedigplVEHTYEVINNgPS----TVSGASLEISWPYE 366

                          410       420
                   ....*....|....*....|....*
gi 1239906661  883 HSEGpithKW-----NVEMEPPVTC 902
Cdd:pfam08441  367 LSNG----KWllyllDVQGQGKGEC 387
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 59-221 1.23e-27

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 110.01  E-value: 1.23e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   59 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKL--SNSSYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL-- 134
Cdd:cd01472      1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLdiGPDGVRVGVVQYSDDPRTEFYLNTY---RSKDDVLEAVKNLRYIgg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  135 -TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATDRANIDSAKD----IIRYIIGIGKHfatkrSQETLHQFASK 209
Cdd:cd01472     78 gTNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELkqagIEVFAVGVKNA-----DEEELKQIASD 152

                          170
                   ....*....|..
gi 1239906661  210 PAEEFVKILDTF 221
Cdd:cd01472    153 PKELYVFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 60-221 9.04e-26

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


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 104.68  E-value: 9.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   60 DLVFLFDGSMSLQQDEFQKILDFMKDVMK--KLSNSSYQFAAVQFSTDCKTEFNFLDYVKVKNpdvLLGKVVHMRLL--- 134
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEafEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKED---VLAAIKNLPYKggn 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  135 TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATDraNIDSAKDIIR------YIIGIGKHFAtkrsqETLHQFAS 208
Cdd:cd01482     79 TRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQD--DVELPARVLRnlgvnvFAVGVKDADE-----SELKMIAS 151

                          170
                   ....*....|...
gi 1239906661  209 KPAEEFVKILDTF 221
Cdd:cd01482    152 KPSETHVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 57-235 1.31e-19

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: 88.98  E-value: 1.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   57 GNVDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSNS--SYQFAAVQFSTDCKTEFNFLDYVKVKNPDVLLGKVVHMRLL 134
Cdd:cd01475      1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGpdATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  135 TNTFGAINYVAREVFRQDLGARPDAT---KVLIIITDGEATDRANIDSAK----DIIRYIIGIGkhfatKRSQETLHQFA 207
Cdd:cd01475     81 TMTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKaralGIEMFAVGVG-----RADEEELREIA 155

                          170       180
                   ....*....|....*....|....*...
gi 1239906661  208 SKPAEEFVKILDTFEKLKDLFTELQKKI 235
Cdd:cd01475    156 SEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 59-215 4.13e-16

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 76.84  E-value: 4.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   59 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSNSS--YQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL-- 134
Cdd:cd00198      1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTD---TDKADLLEAIDALKKGlg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  135 --TNTFGAINYVAREVFRQdlgARPDATKVLIIITDGEATD-----RANIDSAKD--IIRYIIGIGKHFATkrsqETLHQ 205
Cdd:cd00198     78 ggTNIGAALRLALELLKSA---KRPNARRVIILLTDGEPNDgpellAEAARELRKlgITVYTIGIGDDANE----DELKE 150

                          170
                   ....*....|
gi 1239906661  206 FASKPAEEFV 215
Cdd:cd00198    151 IADKTTGGAV 160
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 60-173 6.76e-14

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 70.43  E-value: 6.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   60 DLVFLFDGSMSLQQDEFQKILDFMKDVMKKLS--NSSYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLLT-- 135
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTH---STKADVLGAVRRLRLRGgs 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1239906661  136 --NTFGAINYVAREVFRQDLGARPD--ATKVLIIITDGEATD 173
Cdd:cd01481     79 qlNTGSALDYVVKNLFTKSAGSRIEegVPQFLVLITGGKSQD 120
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 421-473 5.84e-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: 64.32  E-value: 5.84e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1239906661   421 PLGRFGAAITALTDINGDGLVDVAVGAPLE----EKGAVYIFNGQHGGLSPQPSQRI 473
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 60-204 2.51e-11

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 63.19  E-value: 2.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   60 DLVFLFDGSMSLQqDEFQKILDFMKDVMKKLSNSSY--QFAAVQFSTDCKT--EFNFldyVKVKNPDVLLGKVVHMRLL- 134
Cdd:cd01476      2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTatRVALITYSGRGRQrvRFNL---PKHNDGEELLEKVDNLRFIg 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239906661  135 --TNTFGAINYvAREVFRQDLGARPDATKVLIIITDGEATDraNIDSAKDIIR-----YIIGIGKHFATKRSQETLH 204
Cdd:cd01476     78 gtTATGAAIEV-ALQQLDPSEGRREGIPKVVVVLTDGRSHD--DPEKQARILRavpniETFAVGTGDPGTVDTEELH 151
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 360-407 2.44e-08

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 51.22  E-value: 2.44e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1239906661   360 IGSYFGGELCGV-DIDQDGETELLlIGAPLFYGEQRGGRVFIYQRKQLG 407
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 57-210 9.92e-08

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 53.16  E-value: 9.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   57 GNVDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLS--------NSSYQFAAVQFSTDCKTEFNFLDYvkVKNPDVLLGKV 128
Cdd:cd01480      1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLkdyyrkdpAGSWRVGVVQYSDQQEVEAGFLRD--IRNYTSLKEAV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  129 VHMRLL---TNTFGAINYVAREVFRqdlGARPDATKVLIIITDGE---ATDRANIDSAKDIIRYIIGIGKHFATKRSQET 202
Cdd:cd01480     79 DNLEYIgggTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHsdgSPDGGIEKAVNEADHLGIKIFFVAVGSQNEEP 155


                   ....*...
gi 1239906661  203 LHQFASKP 210
Cdd:cd01480    156 LSRIACDG 163
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 57-234 1.02e-07

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 53.28  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   57 GNVDLVFLFDGSMSLQqDEFQKILDFMKDVMKKLSNSSYQFAAVQFSTDCKTEFNFLDYVKVKNPDVLLGKVVHMRLLTN 136
Cdd:cd01474      3 GHFDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTY 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  137 TFGAINYVAREVFRQDLGARPDAtKVLIIITDGE--------ATDRANIDSAKDIIRYIIGIgkhfaTKRSQETLHQFAS 208
Cdd:cd01474     82 IHEGLENANEQIFNRNGGGRETV-SVIIALTDGQlllnghkyPEHEAKLSRKLGAIVYCVGV-----TDFLKSQLINIAD 155

                          170       180
                   ....*....|....*....|....*.
gi 1239906661  209 KPAEEFvKILDTFEKLKDLFTELQKK 234
Cdd:cd01474    156 SKEYVF-PVTSGFQALSGIIESVVKK 180
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 425-458 3.06e-07

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 47.51  E-value: 3.06e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1239906661  425 FGAAItALTDINGDGLVDVAVGAPLE---EKGAVYIF 458
Cdd:pfam01839    1 FGYSV-AVGDLNGDGYADLAVGAPGEggaGAGAVYVL 36
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 59-191 1.76e-06

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 49.69  E-value: 1.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   59 VDLVFLFDGSMSL-QQDEFQKILDFMKDVMKKL--SNSSYQFAAVQFSTDCKTEFNFLDYvKVKNPDVLLGKVVHMRLL- 134
Cdd:cd01471      1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLniSPDEINLYLVTFSTNAKELIRLSSP-NSTNKDLALNAIRALLSLy 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239906661  135 -----TNTFGAINyVAREVFRQDLGARPDATKVLIIITDGEATDR------ANIDSAKDIIRYIIGIG 191
Cdd:cd01471     80 ypngsTNTTSALL-VVEKHLFDTRGNRENAPQLVIIMTDGIPDSKfrtlkeARKLRERGVIIAVLGVG 146
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 61-207 5.96e-05

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


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 46.15  E-value: 5.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661   61 LVFLFD--GSMSLQQDEFQK-ILDFMKDVMKKlsnsSYQFAAVQFST----------DCKTEFNFLDYVKVKNPDVLLGK 127
Cdd:TIGR03436   56 VGLVIDtsGSMRNDLDRARAaAIRFLKTVLRP----NDRVFVVTFNTrlrllqdftsDPRLLEAALNRLKPPLRTDYNSS 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239906661  128 VVHMRLL--TNTFGAINYVAREVFRQDLGARPDaTKVLIIITDG----------EATDRANidsAKDIIRYIIGIGKHF- 194
Cdd:TIGR03436  132 GAFVRDGggTALYDAITLAALEQLANALAGIPG-RKALIVISDGgdnrsrdtleRAIDAAQ---RADVAIYSIDARGLRa 207

                          170       180
                   ....*....|....*....|.
gi 1239906661  195 --------ATKRSQETLHQFA 207
Cdd:TIGR03436  208 pdlgagakAGLGGPEALERLA 228
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 483-528 8.99e-05

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 41.21  E-value: 8.99e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1239906661   483 QWFGRSIHGVKDLGGDGLTDVAVGA--------EGQVIVLSSRPVVDILTHISF 528
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 434-505 8.99e-05

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


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 41.44  E-value: 8.99e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239906661  434 DINGDGLVDVAVGAPleEKGAVYIFNGQhGGLSPQPSQRIEGIQVFSGIQWFgrsihgvkDLGGDGLTDVAV 505
Cdd:pfam13517    1 DLDGDGKLDLVVAND--GGLRLYLNNGD-GTFTFITSVSLGGGGGGLSVAVG--------DLDGDGRLDLLV 61
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 364-401 4.49e-04

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 38.65  E-value: 4.49e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1239906661  364 FGGELCGVDIDQDGETElLLIGAPlFYGEQRGGRVFIY 401
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAP-GEGGAGAGAVYVL 36
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1017-1031 3.02e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 35.94  E-value: 3.02e-03
                           10
                   ....*....|....*
gi 1239906661 1017 KLGFFKRNLKEKMEA 1031
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 372-445 3.04e-03

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


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 36.82  E-value: 3.04e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1239906661  372 DIDQDGETELLLIGAplfygeqrgGRVFIYQRKQLG-FEAVSELQGEPGYPLGRFGAAitaltDINGDGLVDVAV 445
Cdd:pfam13517    1 DLDGDGKLDLVVAND---------GGLRLYLNNGDGtFTFITSVSLGGGGGGLSVAVG-----DLDGDGRLDLLV 61
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 306-355 8.50e-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: 8.50e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1239906661   306 GYLGYTVTW---LYSRGLTSLLAaGAPRYQH---VGRVVLFQESKDKEHWSQIQKI 355
Cdd:smart00191    3 SYFGYSVAGvgdVNGDGYPDLLV-GAPRANDageTGAVYVYFGSSGGGNSIPLQNL 57
 
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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