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Conserved domains on  [gi|73958405|ref|XP_547024|]
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integrin alpha-L isoform X1 [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 ...
 153-321 2.41e-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: 2.41e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  153 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSN--SSYQFAAVQFSTDCKTEFNFLDYVKVKNPDVLLGKVVHMRLLTN 230
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  231 TFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD----RANIDSAK--DIIRYIIGIGKHFATKRSQETLHQFASKP 304
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                        170
                 ....*....|....*..
gi 73958405  305 AEEFVKILDTFEKLKDL 321
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 ...
 611-996 1.13e-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: 127.05  E-value: 1.13e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    611 RPVVDILTHISFSPAEIPVHEVECSHSTSNKKkeGVNITVCFQVKPLTLqFRGRLVANliYTLQLD---GHRTRSRGLFP 687
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS--CFTVRACFSYTGKPI-PNPSLVLN--YELELDrqkKKGLPPRVLFL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    688 GGRQ-ELSGNIAVTR--DWSCIKLWFHFPVCIQDLISPINVSLNFSLweeEETPRNKRALDrDIRPIL---RPLphVANT 761
Cdd:pfam08441   76 DSQQpSLTGTLVLLSqgRKVCRTTKAYLRDEFRDKLSPIVISLNYSL---RVDPRAPSDLP-GLKPILdqnQPS--TVQE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    762 EIPFEKNCGEDKKCEADLGLSFSP---AGSRVLRLIPSASLSVELILSNLREDAYSVHLNLSFPQGLSFRKVEMLKPHSQ 838
Cdd:pfam08441  150 QANFLKDCGEDNVCVPDLQLSAKFdsrESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    839 IpvSCEelpevAKLMN--RIVSCNVSSPiFRAGSVVAIQVMF---HMLLNsswGDSVELHANVSCHNEDSGLLEnnlatt 913
Cdd:pfam08441  230 L--SCT-----AKKENstRQVVCDLGNP-MKRGTQVTFGLRFsvsGLELS---TEELSFDLQIRSTNEQNSNSN------ 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    914 tiPVLYPINILTEDK------ENSTLYVGFTPKG-PKMYF---------VEHFYQVRIQ-PSiydhKVPALEALIGVPVS 976
Cdd:pfam08441  293 --PVSLKVPVVAEAQlslsgvSKPDQVVGGSVKGeSAMKPrseedigplVEHTYEVINNgPS----TVSGASLEISWPYE 366

                          410       420
                   ....*....|....*....|....*
gi 73958405    977 HSEGpithKW-----NVEMEPPVTC 996
Cdd:pfam08441  367 LSNG----KWllyllDVQGQGKGEC 387
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 515-567 1.10e-12

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 63.55  E-value: 1.10e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 73958405     515 PLGRFGAAITALTDINGDGLVDVAVGAPLE----EKGAVYIFNGQHGGLSPQPSQRI 567
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 454-501 4.42e-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: 50.84  E-value: 4.42e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 73958405     454 IGSYFGGELCGV-DIDQDGETELLlIGAPLFYGEQRGGRVFIYQRKQLG 501
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 577-622 1.48e-04

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 40.82  E-value: 1.48e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 73958405     577 QWFGRSIHGVKDLGGDGLTDVAVGA--------EGQVIVLSSRPVVDILTHISF 622
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1111-1125 2.88e-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: 2.88e-03
                           10
                   ....*....|....*
gi 73958405   1111 KLGFFKRNLKEKMEA 1125
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 153-321 2.41e-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: 2.41e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  153 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSN--SSYQFAAVQFSTDCKTEFNFLDYVKVKNPDVLLGKVVHMRLLTN 230
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  231 TFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD----RANIDSAK--DIIRYIIGIGKHFATKRSQETLHQFASKP 304
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                        170
                 ....*....|....*..
gi 73958405  305 AEEFVKILDTFEKLKDL 321
Cdd:cd01469  161 PEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
154-324 6.36e-41

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 148.58  E-value: 6.36e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    154 DLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSNS--SYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL--- 228
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGpdGTRVGLVQYSSDVRTEFPLNDY---SSKEELLSAVDNLRYLggg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    229 -TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD---RANIDSAKD--IIRYIIGIGKHFAtkrsqETLHQFAS 302
Cdd:pfam00092   78 tTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgdpEEVARELKSagVTVFAVGVGNADD-----EELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 73958405    303 KPAEEFVKILDTFEKLKDLFTE 324
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 154-318 1.33e-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: 121.79  E-value: 1.33e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405     154 DLVFLFDGSMSLQQDEFQKILDFMKDVMKKL--SNSSYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL--- 228
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDS---RSKDALLEALASLSYKlgg 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405     229 -TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD-----RANIDSAKD--IIRYIIGIGKHFatkrSQETLHQF 300
Cdd:smart00327   78 gTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkdlLKAAKELKRsgVKVFVVGVGNDV----DEEELKKL 153

                           170
                    ....*....|....*...
gi 73958405     301 ASKPAEEFVKILDTFEKL 318
Cdd:smart00327  154 ASAPGGVYVFLPELLDLL 171
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 611-996 1.13e-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: 127.05  E-value: 1.13e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    611 RPVVDILTHISFSPAEIPVHEVECSHSTSNKKkeGVNITVCFQVKPLTLqFRGRLVANliYTLQLD---GHRTRSRGLFP 687
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS--CFTVRACFSYTGKPI-PNPSLVLN--YELELDrqkKKGLPPRVLFL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    688 GGRQ-ELSGNIAVTR--DWSCIKLWFHFPVCIQDLISPINVSLNFSLweeEETPRNKRALDrDIRPIL---RPLphVANT 761
Cdd:pfam08441   76 DSQQpSLTGTLVLLSqgRKVCRTTKAYLRDEFRDKLSPIVISLNYSL---RVDPRAPSDLP-GLKPILdqnQPS--TVQE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    762 EIPFEKNCGEDKKCEADLGLSFSP---AGSRVLRLIPSASLSVELILSNLREDAYSVHLNLSFPQGLSFRKVEMLKPHSQ 838
Cdd:pfam08441  150 QANFLKDCGEDNVCVPDLQLSAKFdsrESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    839 IpvSCEelpevAKLMN--RIVSCNVSSPiFRAGSVVAIQVMF---HMLLNsswGDSVELHANVSCHNEDSGLLEnnlatt 913
Cdd:pfam08441  230 L--SCT-----AKKENstRQVVCDLGNP-MKRGTQVTFGLRFsvsGLELS---TEELSFDLQIRSTNEQNSNSN------ 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    914 tiPVLYPINILTEDK------ENSTLYVGFTPKG-PKMYF---------VEHFYQVRIQ-PSiydhKVPALEALIGVPVS 976
Cdd:pfam08441  293 --PVSLKVPVVAEAQlslsgvSKPDQVVGGSVKGeSAMKPrseedigplVEHTYEVINNgPS----TVSGASLEISWPYE 366

                          410       420
                   ....*....|....*....|....*
gi 73958405    977 HSEGpithKW-----NVEMEPPVTC 996
Cdd:pfam08441  367 LSNG----KWllyllDVQGQGKGEC 387
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 515-567 1.10e-12

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 63.55  E-value: 1.10e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 73958405     515 PLGRFGAAITALTDINGDGLVDVAVGAPLE----EKGAVYIFNGQHGGLSPQPSQRI 567
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 454-501 4.42e-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: 50.84  E-value: 4.42e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 73958405     454 IGSYFGGELCGV-DIDQDGETELLlIGAPLFYGEQRGGRVFIYQRKQLG 501
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 ...
 519-552 4.01e-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: 47.12  E-value: 4.01e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 73958405    519 FGAAItALTDINGDGLVDVAVGAPLE---EKGAVYIF 552
Cdd:pfam01839    1 FGYSV-AVGDLNGDGYADLAVGAPGEggaGAGAVYVL 36
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 155-301 6.57e-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: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    155 LVFLFD--GSMSLQQDEFQK-ILDFMKDVMKKlsnsSYQFAAVQFST----------DCKTEFNFLDYVKVKNPDVLLGK 221
Cdd:TIGR03436   56 VGLVIDtsGSMRNDLDRARAaAIRFLKTVLRP----NDRVFVVTFNTrlrllqdftsDPRLLEAALNRLKPPLRTDYNSS 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    222 VVHMRLL--TNTFGAINYVAREVFRQDLGARPDaTKVLIIITDG----------EATDRANidsAKDIIRYIIGIGKHF- 288
Cdd:TIGR03436  132 GAFVRDGggTALYDAITLAALEQLANALAGIPG-RKALIVISDGgdnrsrdtleRAIDAAQ---RADVAIYSIDARGLRa 207

                          170       180
                   ....*....|....*....|.
gi 73958405    289 --------ATKRSQETLHQFA 301
Cdd:TIGR03436  208 pdlgagakAGLGGPEALERLA 228
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 577-622 1.48e-04

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 40.82  E-value: 1.48e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 73958405     577 QWFGRSIHGVKDLGGDGLTDVAVGA--------EGQVIVLSSRPVVDILTHISF 622
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 458-495 5.83e-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: 38.26  E-value: 5.83e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 73958405    458 FGGELCGVDIDQDGETElLLIGAPlFYGEQRGGRVFIY 495
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAP-GEGGAGAGAVYVL 36
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1111-1125 2.88e-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: 2.88e-03
                           10
                   ....*....|....*
gi 73958405   1111 KLGFFKRNLKEKMEA 1125
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
 
Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 153-321 2.41e-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: 2.41e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  153 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSN--SSYQFAAVQFSTDCKTEFNFLDYVKVKNPDVLLGKVVHMRLLTN 230
Cdd:cd01469    1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  231 TFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD----RANIDSAK--DIIRYIIGIGKHFATKRSQETLHQFASKP 304
Cdd:cd01469   81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDdpllKDVIPQAEreGIIRYAIGVGGHFQRENSREELKTIASKP 160

                        170
                 ....*....|....*..
gi 73958405  305 AEEFVKILDTFEKLKDL 321
Cdd:cd01469  161 PEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
154-324 6.36e-41

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 148.58  E-value: 6.36e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    154 DLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSNS--SYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL--- 228
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGpdGTRVGLVQYSSDVRTEFPLNDY---SSKEELLSAVDNLRYLggg 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    229 -TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD---RANIDSAKD--IIRYIIGIGKHFAtkrsqETLHQFAS 302
Cdd:pfam00092   78 tTNTGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDgdpEEVARELKSagVTVFAVGVGNADD-----EELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 73958405    303 KPAEEFVKILDTFEKLKDLFTE 324
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 154-318 1.33e-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: 121.79  E-value: 1.33e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405     154 DLVFLFDGSMSLQQDEFQKILDFMKDVMKKL--SNSSYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL--- 228
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDS---RSKDALLEALASLSYKlgg 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405     229 -TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATD-----RANIDSAKD--IIRYIIGIGKHFatkrSQETLHQF 300
Cdd:smart00327   78 gTNLGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDgpkdlLKAAKELKRsgVKVFVVGVGNDV----DEEELKKL 153

                           170
                    ....*....|....*...
gi 73958405     301 ASKPAEEFVKILDTFEKL 318
Cdd:smart00327  154 ASAPGGVYVFLPELLDLL 171
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 153-309 2.35e-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: 120.86  E-value: 2.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  153 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSNS--SYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL-- 228
Cdd:cd01450    1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGpdKTRVGLVQYSDDVRVEFSLNDY---KSKDDLLKAVKNLKYLgg 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  229 --TNTFGAINYVAREVFRQDlGARPDATKVLIIITDGEATDRANIDSAKDIIR------YIIGIGKHfatkrSQETLHQF 300
Cdd:cd01450   78 ggTNTGKALQYALEQLFSES-NARENVPKVIIVLTDGRSDDGGDPKEAAAKLKdegikvFVVGVGPA-----DEEELREI 151


                 ....*....
gi 73958405  301 ASKPAEEFV 309
Cdd:cd01450  152 ASCPSERHV 160
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 611-996 1.13e-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: 127.05  E-value: 1.13e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    611 RPVVDILTHISFSPAEIPVHEVECSHSTSNKKkeGVNITVCFQVKPLTLqFRGRLVANliYTLQLD---GHRTRSRGLFP 687
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS--CFTVRACFSYTGKPI-PNPSLVLN--YELELDrqkKKGLPPRVLFL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    688 GGRQ-ELSGNIAVTR--DWSCIKLWFHFPVCIQDLISPINVSLNFSLweeEETPRNKRALDrDIRPIL---RPLphVANT 761
Cdd:pfam08441   76 DSQQpSLTGTLVLLSqgRKVCRTTKAYLRDEFRDKLSPIVISLNYSL---RVDPRAPSDLP-GLKPILdqnQPS--TVQE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    762 EIPFEKNCGEDKKCEADLGLSFSP---AGSRVLRLIPSASLSVELILSNLREDAYSVHLNLSFPQGLSFRKVEMLKPHSQ 838
Cdd:pfam08441  150 QANFLKDCGEDNVCVPDLQLSAKFdsrESDEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    839 IpvSCEelpevAKLMN--RIVSCNVSSPiFRAGSVVAIQVMF---HMLLNsswGDSVELHANVSCHNEDSGLLEnnlatt 913
Cdd:pfam08441  230 L--SCT-----AKKENstRQVVCDLGNP-MKRGTQVTFGLRFsvsGLELS---TEELSFDLQIRSTNEQNSNSN------ 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    914 tiPVLYPINILTEDK------ENSTLYVGFTPKG-PKMYF---------VEHFYQVRIQ-PSiydhKVPALEALIGVPVS 976
Cdd:pfam08441  293 --PVSLKVPVVAEAQlslsgvSKPDQVVGGSVKGeSAMKPrseedigplVEHTYEVINNgPS----TVSGASLEISWPYE 366

                          410       420
                   ....*....|....*....|....*
gi 73958405    977 HSEGpithKW-----NVEMEPPVTC 996
Cdd:pfam08441  367 LSNG----KWllyllDVQGQGKGEC 387
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 153-315 1.02e-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: 110.40  E-value: 1.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  153 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKL--SNSSYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL-- 228
Cdd:cd01472    1 ADIVFLVDGSESIGLSNFNLVKDFVKRVVERLdiGPDGVRVGVVQYSDDPRTEFYLNTY---RSKDDVLEAVKNLRYIgg 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  229 -TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATDRANIDSAKD----IIRYIIGIGKHfatkrSQETLHQFASK 303
Cdd:cd01472   78 gTNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELkqagIEVFAVGVKNA-----DEEELKQIASD 152

                        170
                 ....*....|..
gi 73958405  304 PAEEFVKILDTF 315
Cdd:cd01472  153 PKELYVFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 154-315 7.42e-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: 105.06  E-value: 7.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  154 DLVFLFDGSMSLQQDEFQKILDFMKDVMK--KLSNSSYQFAAVQFSTDCKTEFNFLDYVKVKNpdvLLGKVVHMRLL--- 228
Cdd:cd01482    2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEafEIGPDGVQVGLVQYSDDPRTEFDLNAYTSKED---VLAAIKNLPYKggn 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  229 TNTFGAINYVAREVFRQDLGARPDATKVLIIITDGEATDraNIDSAKDIIR------YIIGIGKHFAtkrsqETLHQFAS 302
Cdd:cd01482   79 TRTGKALTHVREKNFTPDAGARPGVPKVVILITDGKSQD--DVELPARVLRnlgvnvFAVGVKDADE-----SELKMIAS 151

                        170
                 ....*....|...
gi 73958405  303 KPAEEFVKILDTF 315
Cdd:cd01482  152 KPSETHVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 151-329 1.44e-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: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  151 GNVDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSNS--SYQFAAVQFSTDCKTEFNFLDYVKVKNPDVLLGKVVHMRLL 228
Cdd:cd01475    1 GPTDLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGpdATRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  229 TNTFGAINYVAREVFRQDLGARPDAT---KVLIIITDGEATDRANIDSAK----DIIRYIIGIGkhfatKRSQETLHQFA 301
Cdd:cd01475   81 TMTGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRPQDDVSEVAAKaralGIEMFAVGVG-----RADEEELREIA 155

                        170       180
                 ....*....|....*....|....*...
gi 73958405  302 SKPAEEFVKILDTFEKLKDLFTELQKKI 329
Cdd:cd01475  156 SEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 153-309 3.66e-16

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 77.22  E-value: 3.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  153 VDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLSNSS--YQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLL-- 228
Cdd:cd00198    1 ADIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTD---TDKADLLEAIDALKKGlg 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  229 --TNTFGAINYVAREVFRQdlgARPDATKVLIIITDGEATD-----RANIDSAKD--IIRYIIGIGKHFATkrsqETLHQ 299
Cdd:cd00198   78 ggTNIGAALRLALELLKSA---KRPNARRVIILLTDGEPNDgpellAEAARELRKlgITVYTIGIGDDANE----DELKE 150

                        170
                 ....*....|
gi 73958405  300 FASKPAEEFV 309
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 ...
 154-267 6.73e-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: 70.82  E-value: 6.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  154 DLVFLFDGSMSLQQDEFQKILDFMKDVMKKLS--NSSYQFAAVQFSTDCKTEFNFLDYvkvKNPDVLLGKVVHMRLLT-- 229
Cdd:cd01481    2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTH---STKADVLGAVRRLRLRGgs 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 73958405  230 --NTFGAINYVAREVFRQDLGARPD--ATKVLIIITDGEATD 267
Cdd:cd01481   79 qlNTGSALDYVVKNLFTKSAGSRIEegVPQFLVLITGGKSQD 120
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 515-567 1.10e-12

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 63.55  E-value: 1.10e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 73958405     515 PLGRFGAAITALTDINGDGLVDVAVGAPLE----EKGAVYIFNGQHGGLSPQPSQRI 567
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRAndagETGAVYVYFGSSGGGNSIPLQNL 57
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 154-298 2.31e-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: 2.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  154 DLVFLFDGSMSLQqDEFQKILDFMKDVMKKLSNSSY--QFAAVQFSTDCKT--EFNFldyVKVKNPDVLLGKVVHMRLL- 228
Cdd:cd01476    2 DLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEIGPTatRVALITYSGRGRQrvRFNL---PKHNDGEELLEKVDNLRFIg 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73958405  229 --TNTFGAINYvAREVFRQDLGARPDATKVLIIITDGEATDraNIDSAKDIIR-----YIIGIGKHFATKRSQETLH 298
Cdd:cd01476   78 gtTATGAAIEV-ALQQLDPSEGRREGIPKVVVVLTDGRSHD--DPEKQARILRavpniETFAVGTGDPGTVDTEELH 151
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 454-501 4.42e-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: 50.84  E-value: 4.42e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 73958405     454 IGSYFGGELCGV-DIDQDGETELLlIGAPLFYGEQRGGRVFIYQRKQLG 501
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGG 48
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 151-328 1.03e-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: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  151 GNVDLVFLFDGSMSLQqDEFQKILDFMKDVMKKLSNSSYQFAAVQFSTDCKTEFNFLDYVKVKNPDVLLGKVVHMRLLTN 230
Cdd:cd01474    3 GHFDLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  231 TFGAINYVAREVFRQDLGARPDAtKVLIIITDGE--------ATDRANIDSAKDIIRYIIGIgkhfaTKRSQETLHQFAS 302
Cdd:cd01474   82 IHEGLENANEQIFNRNGGGRETV-SVIIALTDGQlllnghkyPEHEAKLSRKLGAIVYCVGV-----TDFLKSQLINIAD 155

                        170       180
                 ....*....|....*....|....*.
gi 73958405  303 KPAEEFvKILDTFEKLKDLFTELQKK 328
Cdd:cd01474  156 SKEYVF-PVTSGFQALSGIIESVVKK 180
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 151-304 1.09e-07

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 53.16  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  151 GNVDLVFLFDGSMSLQQDEFQKILDFMKDVMKKLS--------NSSYQFAAVQFSTDCKTEFNFLDYvkVKNPDVLLGKV 222
Cdd:cd01480    1 GPVDITFVLDSSESVGLQNFDITKNFVKRVAERFLkdyyrkdpAGSWRVGVVQYSDQQEVEAGFLRD--IRNYTSLKEAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  223 VHMRLL---TNTFGAINYVAREVFRqdlGARPDATKVLIIITDGE---ATDRANIDSAKDIIRYIIGIGKHFATKRSQET 296
Cdd:cd01480   79 DNLEYIgggTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHsdgSPDGGIEKAVNEADHLGIKIFFVAVGSQNEEP 155


                 ....*...
gi 73958405  297 LHQFASKP 304
Cdd:cd01480  156 LSRIACDG 163
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 519-552 4.01e-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: 47.12  E-value: 4.01e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 73958405    519 FGAAItALTDINGDGLVDVAVGAPLE---EKGAVYIF 552
Cdd:pfam01839    1 FGYSV-AVGDLNGDGYADLAVGAPGEggaGAGAVYVL 36
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 153-285 1.93e-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: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405  153 VDLVFLFDGSMSL-QQDEFQKILDFMKDVMKKL--SNSSYQFAAVQFSTDCKTEFNFLDYvKVKNPDVLLGKVVHMRLL- 228
Cdd:cd01471    1 LDLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLniSPDEINLYLVTFSTNAKELIRLSSP-NSTNKDLALNAIRALLSLy 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73958405  229 -----TNTFGAINyVAREVFRQDLGARPDATKVLIIITDGEATDR------ANIDSAKDIIRYIIGIG 285
Cdd:cd01471   80 ypngsTNTTSALL-VVEKHLFDTRGNRENAPQLVIIMTDGIPDSKfrtlkeARKLRERGVIIAVLGVG 146
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 155-301 6.57e-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: 6.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    155 LVFLFD--GSMSLQQDEFQK-ILDFMKDVMKKlsnsSYQFAAVQFST----------DCKTEFNFLDYVKVKNPDVLLGK 221
Cdd:TIGR03436   56 VGLVIDtsGSMRNDLDRARAaAIRFLKTVLRP----NDRVFVVTFNTrlrllqdftsDPRLLEAALNRLKPPLRTDYNSS 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73958405    222 VVHMRLL--TNTFGAINYVAREVFRQDLGARPDaTKVLIIITDG----------EATDRANidsAKDIIRYIIGIGKHF- 288
Cdd:TIGR03436  132 GAFVRDGggTALYDAITLAALEQLANALAGIPG-RKALIVISDGgdnrsrdtleRAIDAAQ---RADVAIYSIDARGLRa 207

                          170       180
                   ....*....|....*....|.
gi 73958405    289 --------ATKRSQETLHQFA 301
Cdd:TIGR03436  208 pdlgagakAGLGGPEALERLA 228
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 528-599 9.32e-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: 9.32e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73958405    528 DINGDGLVDVAVGAPleEKGAVYIFNGQhGGLSPQPSQRIEGIQVFSGIQWFgrsihgvkDLGGDGLTDVAV 599
Cdd:pfam13517    1 DLDGDGKLDLVVAND--GGLRLYLNNGD-GTFTFITSVSLGGGGGGLSVAVG--------DLDGDGRLDLLV 61
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 577-622 1.48e-04

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 40.82  E-value: 1.48e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 73958405     577 QWFGRSIHGVKDLGGDGLTDVAVGA--------EGQVIVLSSRPVVDILTHISF 622
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprandageTGAVYVYFGSSGGGNSIPLQN 56
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 458-495 5.83e-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: 38.26  E-value: 5.83e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 73958405    458 FGGELCGVDIDQDGETElLLIGAPlFYGEQRGGRVFIY 495
Cdd:pfam01839    1 FGYSVAVGDLNGDGYAD-LAVGAP-GEGGAGAGAVYVL 36
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1111-1125 2.88e-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: 2.88e-03
                           10
                   ....*....|....*
gi 73958405   1111 KLGFFKRNLKEKMEA 1125
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 466-539 3.09e-03

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


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 37.20  E-value: 3.09e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 73958405    466 DIDQDGETELLLIGAplfygeqrgGRVFIYQRKQLG-FEAVSELQGEPGYPLGRFGAAitaltDINGDGLVDVAV 539
Cdd:pfam13517    1 DLDGDGKLDLVVAND---------GGLRLYLNNGDGtFTFITSVSLGGGGGGLSVAVG-----DLDGDGRLDLLV 61
 
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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