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Conserved domains on  [gi|1958649268|ref|XP_038945483|]
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integrin alpha-D isoform X1 [Rattus norvegicus]

Protein Classification

integrin alpha( domain architecture ID 11546373)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 1-176 1.08e-83

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: 267.68  E-value: 1.08e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    1 MDIAFLIDGSGSINQRDFAQMKDFVKALMGEF--ASTSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPIVQLQGLTY 78
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLdiGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   79 TATGIRTVVEELFHSKNGSRKSAKKILLVITDGQKYRDPLEySDVIPAADKAGIIRYAIGVGDAFQEPTALKELNTIGSA 158
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                          170
                   ....*....|....*...
gi 1958649268  159 PPQDHVFKVGNFAALRSI 176
Cdd:cd01469    160 PPEEHFFNVTDFAALKDI 177
Integrin_alpha2 super family cl26747
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 472-771 3.23e-29

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: 122.04  E-value: 3.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268  472 VELSIRFAPMEVAKAVYQCwERTPTVLEAGEATVCLTVHkGSPDLLGNVqgSVRYDLALDPGR---LISRAIFDETKNCT 548
Cdd:pfam08441    6 VSASLQVEPNSINPEKKNC-TLTGTPVSCFTVRACFSYT-GKPIPNPSL--VLNYELELDRQKkkgLPPRVLFLDSQQPS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268  549 LTGRKTLGLG--DHCETVKLLLPDCVEDAVSPIILRLNFSLVRDSASPRNLH---PVLAVGSQDHITASLPFEKNCKQEL 623
Cdd:pfam08441   82 LTGTLVLLSQgrKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRAPSDLPglkPILDQNQPSTVQEQANFLKDCGEDN 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268  624 LCEGDLGIS--FNFSGLQ-VLVVGGSPELTVTVTVWNEGEDSYGTLVKFYYPAGLSYRRVTGTQQPHQyplrLACEAEPA 700
Cdd:pfam08441  162 VCVPDLQLSakFDSRESDePLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ----LSCTAKKE 237

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958649268  701 AQEdlRSSSCSINHPiFREGAKTTFMITFDVSYKAFLGDRLLLRAKASSEN-NKPDTNKTafQLELPVKYTV 771
Cdd:pfam08441  238 NST--RQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNeQNSNSNPV--SLKVPVVAEA 304
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 305-361 5.33e-11

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: 58.93  E-value: 5.33e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649268   305 IGSYFGASLCSV-DVDRDGSTDLVlIGAPHYYEQTRGGQVSVCPVPGVRGRWQCEATL 361
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 368-409 5.29e-09

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: 53.15  E-value: 5.29e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1958649268   368 PWGRFGVALTVLGDVNGDNLADVAIGAPGEEESR--GAVYIFHG 409
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG 44
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 433-457 1.21e-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: 38.13  E-value: 1.21e-03
                            10        20
                    ....*....|....*....|....*
gi 1958649268   433 QYFGQSLSGGQDLTQDGLVDLAVGA 457
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 974-987 1.96e-03

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


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.32  E-value: 1.96e-03
                           10
                   ....*....|....
gi 1958649268  974 KLGFFKRQYKEMLD 987
Cdd:pfam00357    1 KCGFFKRNYPPQEE 14
 
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 ...
 1-176 1.08e-83

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: 267.68  E-value: 1.08e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    1 MDIAFLIDGSGSINQRDFAQMKDFVKALMGEF--ASTSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPIVQLQGLTY 78
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLdiGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   79 TATGIRTVVEELFHSKNGSRKSAKKILLVITDGQKYRDPLEySDVIPAADKAGIIRYAIGVGDAFQEPTALKELNTIGSA 158
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                          170
                   ....*....|....*...
gi 1958649268  159 PPQDHVFKVGNFAALRSI 176
Cdd:cd01469    160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
2-179 1.97e-46

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 163.99  E-value: 1.97e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMKDFVKALMGEFA--STSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPI-VQLQGLTY 78
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLrYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   79 TATGIRTVVEELFHSKNGSRKSAKKILLVITDGQKYRDplEYSDVIPAADKAGIIRYAIGVGDAFqeptaLKELNTIGSA 158
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVGNAD-----DEELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 1958649268  159 PPQDHVFKVGNFAALRSIQRQ 179
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2-177 1.78e-37

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: 138.74  E-value: 1.78e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268     2 DIAFLIDGSGSINQRDFAQMKDFVKALMGEF--ASTSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPI-VQLQGLTY 78
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    79 TATGIRTVVEELFHSKNGSRKSAKKILLVITDGQKYRDPLEYSDVIPAADKAGIIRYAIGVGDAFQEPtalkELNTIGSA 158
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEE----ELKKLASA 156

                           170
                    ....*....|....*....
gi 1958649268   159 PPQDHVFKVGNFAALRSIQ 177
Cdd:smart00327  157 PGGVYVFLPELLDLLIDLL 175
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 472-771 3.23e-29

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: 122.04  E-value: 3.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268  472 VELSIRFAPMEVAKAVYQCwERTPTVLEAGEATVCLTVHkGSPDLLGNVqgSVRYDLALDPGR---LISRAIFDETKNCT 548
Cdd:pfam08441    6 VSASLQVEPNSINPEKKNC-TLTGTPVSCFTVRACFSYT-GKPIPNPSL--VLNYELELDRQKkkgLPPRVLFLDSQQPS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268  549 LTGRKTLGLG--DHCETVKLLLPDCVEDAVSPIILRLNFSLVRDSASPRNLH---PVLAVGSQDHITASLPFEKNCKQEL 623
Cdd:pfam08441   82 LTGTLVLLSQgrKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRAPSDLPglkPILDQNQPSTVQEQANFLKDCGEDN 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268  624 LCEGDLGIS--FNFSGLQ-VLVVGGSPELTVTVTVWNEGEDSYGTLVKFYYPAGLSYRRVTGTQQPHQyplrLACEAEPA 700
Cdd:pfam08441  162 VCVPDLQLSakFDSRESDePLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ----LSCTAKKE 237

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958649268  701 AQEdlRSSSCSINHPiFREGAKTTFMITFDVSYKAFLGDRLLLRAKASSEN-NKPDTNKTafQLELPVKYTV 771
Cdd:pfam08441  238 NST--RQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNeQNSNSNPV--SLKVPVVAEA 304
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 305-361 5.33e-11

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: 58.93  E-value: 5.33e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649268   305 IGSYFGASLCSV-DVDRDGSTDLVlIGAPHYYEQTRGGQVSVCPVPGVRGRWQCEATL 361
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGGGNSIPLQNL 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2-180 2.60e-09

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 59.18  E-value: 2.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRD-FAQMKDFVKALMGEFASTsTLFSLMQYSNILKTHFTFTEfknilDPQSLVDPIVQLQ--GLTY 78
Cdd:COG1240     94 DVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR-DRVGLVAFGGEAEVLLPLTR-----DREALKRALDELPpgGGTP 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   79 TATGIRTVVEELfhskNGSRKSAKKILLVITDGQKYRDPLEYSDVIPAADKAGIIRYAIGVGDAFQEPTALKELNTIGSA 158
Cdd:COG1240    168 LGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEGLLREIAEATGG 243

                          170       180
                   ....*....|....*....|..
gi 1958649268  159 ppqdHVFKVGNFAALRSIQRQL 180
Cdd:COG1240    244 ----RYFRADDLSELAAIYREI 261
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 368-409 5.29e-09

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: 53.15  E-value: 5.29e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1958649268   368 PWGRFGVALTVLGDVNGDNLADVAIGAPGEEESR--GAVYIFHG 409
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG 44
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 372-407 2.80e-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: 2.80e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958649268  372 FGVALTVlGDVNGDNLADVAIGAPGE-EESRGAVYIF 407
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 3-138 9.87e-07

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: 51.54  E-value: 9.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    3 IAFLIDGSGSI-NQRDFA--QMKDFVKALMGefasTSTLFSLMQYSNILKTHFTFTEFK-------NILDPQS-----LV 67
Cdd:TIGR03436   56 VGLVIDTSGSMrNDLDRAraAAIRFLKTVLR----PNDRVFVVTFNTRLRLLQDFTSDPrlleaalNRLKPPLrtdynSS 131

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958649268   68 DPIVQLQGLTYTATGIRTVVEELFHSKNGSrKSAKKILLVITDGQKYRDPLEYSDVIPAADKAGIIRYAIG 138
Cdd:TIGR03436  132 GAFVRDGGGTALYDAITLAALEQLANALAG-IPGRKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSID 201
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 309-345 6.17e-05

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 40.96  E-value: 6.17e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958649268  309 FGASLCSVDVDRDGSTDLVlIGAPHYYEQtRGGQVSV 345
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLA-VGAPGEGGA-GAGAVYV 35
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 433-457 1.21e-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: 38.13  E-value: 1.21e-03
                            10        20
                    ....*....|....*....|....*
gi 1958649268   433 QYFGQSLSGGQDLTQDGLVDLAVGA 457
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 974-987 1.96e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.32  E-value: 1.96e-03
                           10
                   ....*....|....
gi 1958649268  974 KLGFFKRQYKEMLD 987
Cdd:pfam00357    1 KCGFFKRNYPPQEE 14
 
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 ...
 1-176 1.08e-83

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: 267.68  E-value: 1.08e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    1 MDIAFLIDGSGSINQRDFAQMKDFVKALMGEF--ASTSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPIVQLQGLTY 78
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLdiGPTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   79 TATGIRTVVEELFHSKNGSRKSAKKILLVITDGQKYRDPLEySDVIPAADKAGIIRYAIGVGDAFQEPTALKELNTIGSA 158
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                          170
                   ....*....|....*...
gi 1958649268  159 PPQDHVFKVGNFAALRSI 176
Cdd:cd01469    160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
2-179 1.97e-46

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 163.99  E-value: 1.97e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMKDFVKALMGEFA--STSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPI-VQLQGLTY 78
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLrYLGGGTTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   79 TATGIRTVVEELFHSKNGSRKSAKKILLVITDGQKYRDplEYSDVIPAADKAGIIRYAIGVGDAFqeptaLKELNTIGSA 158
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVGNAD-----DEELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 1958649268  159 PPQDHVFKVGNFAALRSIQRQ 179
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 2-177 1.78e-37

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: 138.74  E-value: 1.78e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268     2 DIAFLIDGSGSINQRDFAQMKDFVKALMGEF--ASTSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPI-VQLQGLTY 78
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdiGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLsYKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    79 TATGIRTVVEELFHSKNGSRKSAKKILLVITDGQKYRDPLEYSDVIPAADKAGIIRYAIGVGDAFQEPtalkELNTIGSA 158
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEE----ELKKLASA 156

                           170
                    ....*....|....*....
gi 1958649268   159 PPQDHVFKVGNFAALRSIQ 177
Cdd:smart00327  157 PGGVYVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1-165 9.08e-33

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: 124.71  E-value: 9.08e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    1 MDIAFLIDGSGSINQRDFAQMKDFVKALMGEF--ASTSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPIVQLQGL-T 77
Cdd:cd01450      1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLdiGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   78 YTATGIRTVVEELFHSKNgSRKSAKKILLVITDGQkyrdPLEYSDVIPAADKA---GIIRYAIGVGDAFQEptalkELNT 154
Cdd:cd01450     81 NTGKALQYALEQLFSESN-ARENVPKVIIVLTDGR----SDDGGDPKEAAAKLkdeGIKVFVVGVGPADEE-----ELRE 150

                          170
                   ....*....|.
gi 1958649268  155 IGSAPPQDHVF 165
Cdd:cd01450    151 IASCPSERHVF 161
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 472-771 3.23e-29

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: 122.04  E-value: 3.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268  472 VELSIRFAPMEVAKAVYQCwERTPTVLEAGEATVCLTVHkGSPDLLGNVqgSVRYDLALDPGR---LISRAIFDETKNCT 548
Cdd:pfam08441    6 VSASLQVEPNSINPEKKNC-TLTGTPVSCFTVRACFSYT-GKPIPNPSL--VLNYELELDRQKkkgLPPRVLFLDSQQPS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268  549 LTGRKTLGLG--DHCETVKLLLPDCVEDAVSPIILRLNFSLVRDSASPRNLH---PVLAVGSQDHITASLPFEKNCKQEL 623
Cdd:pfam08441   82 LTGTLVLLSQgrKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRAPSDLPglkPILDQNQPSTVQEQANFLKDCGEDN 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268  624 LCEGDLGIS--FNFSGLQ-VLVVGGSPELTVTVTVWNEGEDSYGTLVKFYYPAGLSYRRVTGTQQPHQyplrLACEAEPA 700
Cdd:pfam08441  162 VCVPDLQLSakFDSRESDePLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ----LSCTAKKE 237

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958649268  701 AQEdlRSSSCSINHPiFREGAKTTFMITFDVSYKAFLGDRLLLRAKASSEN-NKPDTNKTafQLELPVKYTV 771
Cdd:pfam08441  238 NST--RQVVCDLGNP-MKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNeQNSNSNPV--SLKVPVVAEA 304
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 2-170 1.67e-26

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: 106.54  E-value: 1.67e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMKDFVKALMG--EFASTSTLFSLMQYSNILKTHFTFTEFKNIldpQSLVDPIVQLQ---GL 76
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVErlDIGPDGVRVGVVQYSDDPRTEFYLNTYRSK---DDVLEAVKNLRyigGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   77 TYTATGIRTVVEELFHSKNGSRKSAKKILLVITDGQKYRDPLEYSDVIPaadKAGIIRYAIGVGDAFQEptalkELNTIG 156
Cdd:cd01472     79 TNTGKALKYVRENLFTEASGSREGVPKVLVVITDGKSQDDVEEPAVELK---QAGIEVFAVGVKNADEE-----ELKQIA 150

                          170
                   ....*....|....
gi 1958649268  157 SAPPQDHVFKVGNF 170
Cdd:cd01472    151 SDPKELYVFNVADF 164
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 2-170 2.50e-25

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: 103.14  E-value: 2.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMKDFVKALMGEF--ASTSTLFSLMQYSNILKTHFTFTEFKnilDPQSLVDPIVQLQ---GL 76
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFeiGPDGVQVGLVQYSDDPRTEFDLNAYT---SKEDVLAAIKNLPykgGN 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   77 TYTATGIRTVVEELFHSKNGSRKSAKKILLVITDGqKYRDpleysDVIPAADKA---GIIRYAIGVGDAFQEptalkELN 153
Cdd:cd01482     79 TRTGKALTHVREKNFTPDAGARPGVPKVVILITDG-KSQD-----DVELPARVLrnlGVNVFAVGVKDADES-----ELK 147

                          170
                   ....*....|....*..
gi 1958649268  154 TIGSAPPQDHVFKVGNF 170
Cdd:cd01482    148 MIASKPSETHVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 2-184 4.44e-24

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: 101.69  E-value: 4.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMKDFVkALMGEFASTS---TLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPIVQLQGLTY 78
Cdd:cd01475      4 DLVFLIDSSRSVRPENFELVKQFL-NQIIDSLDVGpdaTRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTM 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   79 TATGIRTVVEELFHSKNGSRKSAK---KILLVITDGQKyRDPLeySDVIPAADKAGIIRYAIGVGDAFQEptalkELNTI 155
Cdd:cd01475     83 TGLAIQYAMNNAFSEAEGARPGSErvpRVGIVVTDGRP-QDDV--SEVAAKARALGIEMFAVGVGRADEE-----ELREI 154

                          170       180
                   ....*....|....*....|....*....
gi 1958649268  156 GSAPPQDHVFKVGNFAALRSIQRQLQEKI 184
Cdd:cd01475    155 ASEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 2-165 6.50e-23

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 96.48  E-value: 6.50e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMKDFVKALMGEF--ASTSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPIV-QLQGLTY 78
Cdd:cd00198      2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsaSPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGTN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   79 TATGIRTVVEELFHSKngsRKSAKKILLVITDGQKYRDPLEYSDVIPAADKAGIIRYAIGVGDAFQEPtalkELNTIGSA 158
Cdd:cd00198     82 IGAALRLALELLKSAK---RPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDANED----ELKEIADK 154


                   ....*..
gi 1958649268  159 PPQDHVF 165
Cdd:cd00198    155 TTGGAVF 161
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 2-176 5.20e-16

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: 77.17  E-value: 5.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQrDFAQMKDFVKALMGEFASTSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPIVQLQGLTYTAT 81
Cdd:cd01474      6 DLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   82 GIRTVVEELFHSKNGSRKSAKKILLvITDGQKYRDPLEYSD-VIPAADKAGIIRYAIGVGDAFQEptalkELNTIGSAPp 160
Cdd:cd01474     85 GLENANEQIFNRNGGGRETVSVIIA-LTDGQLLLNGHKYPEhEAKLSRKLGAIVYCVGVTDFLKS-----QLINIADSK- 157

                          170
                   ....*....|....*..
gi 1958649268  161 qDHVFKV-GNFAALRSI 176
Cdd:cd01474    158 -EYVFPVtSGFQALSGI 173
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 2-165 2.21e-14

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: 71.66  E-value: 2.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRdFAQMKDFVKALMGEF--ASTSTLFSLMQYSNILKTH--FTFTEFKNILDPQSLVDPIVQLQGLT 77
Cdd:cd01476      2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLeiGPTATRVALITYSGRGRQRvrFNLPKHNDGEELLEKVDNLRFIGGTT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   78 YTATGIRtVVEELFHSKNGSRKSAKKILLVITDGQKYRDPLEYSDVIPAAdkAGIIRYAIGVGDafQEPTALKELNTIGS 157
Cdd:cd01476     81 ATGAAIE-VALQQLDPSEGRREGIPKVVVVLTDGRSHDDPEKQARILRAV--PNIETFAVGTGD--PGTVDTEELHSITG 155


                   ....*...
gi 1958649268  158 APpqDHVF 165
Cdd:cd01476    156 NE--DHIF 161
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 305-361 5.33e-11

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: 58.93  E-value: 5.33e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958649268   305 IGSYFGASLCSV-DVDRDGSTDLVlIGAPHYYEQTRGGQVSVCPVPGVRGRWQCEATL 361
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFGSSGGGNSIPLQNL 57
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 2-170 7.94e-11

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: 61.57  E-value: 7.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMKDFVKALMG--EFASTSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDPIvQLQGLT-- 77
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQslDVGPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRL-RLRGGSql 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   78 YTATGIRTVVEELFHSKNGSR--KSAKKILLVITDGQKYRDPLEYSDVIpaaDKAGIIRYAIGVGDAFQEptalkELNTI 155
Cdd:cd01481     81 NTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVAL---KRAGIVPFAIGARNADLA-----ELQQI 152

                          170
                   ....*....|....*
gi 1958649268  156 GSAPpqDHVFKVGNF 170
Cdd:cd01481    153 AFDP--SFVFQVSDF 165
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 2-184 9.11e-11

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: 62.02  E-value: 9.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMKDFVKALMGEF--------ASTSTLFSLMQYSNILKTHFTFTEFKNilDPQSLVDPIVQL 73
Cdd:cd01480      4 DITFVLDSSESVGLQNFDITKNFVKRVAERFlkdyyrkdPAGSWRVGVVQYSDQQEVEAGFLRDIR--NYTSLKEAVDNL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   74 Q---GLTYTATGIRTVVEELFHsknGSRKSAKKILLVITDGQKYRDP---LEysDVIPAADKAGIIRYAIGVGDAFQEPt 147
Cdd:cd01480     82 EyigGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDGSPdggIE--KAVNEADHLGIKIFFVAVGSQNEEP- 155

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1958649268  148 alkeLNTIGSAPPQDHVfkVGNFAALRSIQRQLQEKI 184
Cdd:cd01480    156 ----LSRIACDGKSALY--RENFAELLWSFFIDDETA 186
VWA_2 pfam13519
von Willebrand factor type A domain;
3-108 5.18e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 57.30  E-value: 5.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    3 IAFLIDGSGSINQRD-----FAQMKDFVKALMGEFASTStlFSLMQYSNILKTHFTFTEFKNILdpQSLVDPIVQLQGLT 77
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSLPGDR--VGLVTFGDGPEVLIPLTKDRAKI--LRALRRLEPKGGGT 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958649268   78 YTATGIRTVVEELFHskngSRKSAKKILLVI 108
Cdd:pfam13519   77 NLAAALQLARAALKH----RRKNQPRRIVLI 103
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 2-180 2.60e-09

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 59.18  E-value: 2.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRD-FAQMKDFVKALMGEFASTsTLFSLMQYSNILKTHFTFTEfknilDPQSLVDPIVQLQ--GLTY 78
Cdd:COG1240     94 DVVLVVDASGSMAAENrLEAAKGALLDFLDDYRPR-DRVGLVAFGGEAEVLLPLTR-----DREALKRALDELPpgGGTP 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   79 TATGIRTVVEELfhskNGSRKSAKKILLVITDGQKYRDPLEYSDVIPAADKAGIIRYAIGVGDAFQEPTALKELNTIGSA 158
Cdd:COG1240    168 LGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEGLLREIAEATGG 243

                          170       180
                   ....*....|....*....|..
gi 1958649268  159 ppqdHVFKVGNFAALRSIQRQL 180
Cdd:COG1240    244 ----RYFRADDLSELAAIYREI 261
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 368-409 5.29e-09

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: 53.15  E-value: 5.29e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 1958649268   368 PWGRFGVALTVLGDVNGDNLADVAIGAPGEEESR--GAVYIFHG 409
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG 44
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 372-407 2.80e-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: 2.80e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958649268  372 FGVALTVlGDVNGDNLADVAIGAPGE-EESRGAVYIF 407
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1-140 7.98e-07

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 50.46  E-value: 7.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    1 MDIAFLIDGSGSINqrdFAQMKDFVKALMGEFASTSTL------FSLMQYSNILKTHFTFTEFkNILDPQSLVDPIVQLQ 74
Cdd:cd01471      1 LDLYLLVDGSGSIG---YSNWVTHVVPFLHTFVQNLNIspdeinLYLVTFSTNAKELIRLSSP-NSTNKDLALNAIRALL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958649268   75 ------GLTYTATGIRTVVEELFHSKnGSRKSAKKILLVITDGQKYRDPLEYSDVIPAADKAGIIrYAIGVG 140
Cdd:cd01471     77 slyypnGSTNTTSALLVVEKHLFDTR-GNRENAPQLVIIMTDGIPDSKFRTLKEARKLRERGVII-AVLGVG 146
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 3-138 9.87e-07

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: 51.54  E-value: 9.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    3 IAFLIDGSGSI-NQRDFA--QMKDFVKALMGefasTSTLFSLMQYSNILKTHFTFTEFK-------NILDPQS-----LV 67
Cdd:TIGR03436   56 VGLVIDTSGSMrNDLDRAraAAIRFLKTVLR----PNDRVFVVTFNTRLRLLQDFTSDPrlleaalNRLKPPLrtdynSS 131

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958649268   68 DPIVQLQGLTYTATGIRTVVEELFHSKNGSrKSAKKILLVITDGQKYRDPLEYSDVIPAADKAGIIRYAIG 138
Cdd:TIGR03436  132 GAFVRDGGGTALYDAITLAALEQLANALAG-IPGRKALIVISDGGDNRSRDTLERAIDAAQRADVAIYSID 201
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
2-199 1.60e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 46.84  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMKDFVKALMGEF-----ASTSTLFSLMQYSNILKTHFTFTefknilDPQSLVDPIVQLQGL 76
Cdd:COG4245      7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELrqdpyALETVEVSVITFDGEAKVLLPLT------DLEDFQPPDLSASGG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   77 TYTATGIRTVVEEL-----FHSKNGSRkSAKKILLVITDGQkyrdP--LEYSDVIPAAD----KAGIIRYAIGVGDAFQE 145
Cdd:COG4245     81 TPLGAALELLLDLIerrvqKYTAEGKG-DWRPVVFLITDGE----PtdSDWEAALQRLKdgeaAKKANIFAIGVGPDADT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958649268  146 PTaLKELNTIGSappqdhVFKVGNFAALRsiqrqlqeKIF-AIEGTQSRSSSSFQ 199
Cdd:COG4245    156 EV-LKQLTDPVR------ALDALDGLDFR--------EFFkWLSASVSSVSRSVG 195
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 1-145 2.25e-05

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 47.40  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    1 MDIAFLIDGSGSINQRDFAQMKDFVKALMGEFASTSTlFSLMQYSNILKTHFTFTEfknILDPQSLVDPIVQLQ--GLTY 78
Cdd:COG2304     92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDR-VSIVTFAGDARVLLPPTP---ATDRAKILAAIDRLQagGGTA 167

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   79 TATGIRTVVEELfhsKNGSRKSAKKILLVITDGQ---KYRDPLEYSDVIPAADKAGIIRYAIGVGDAFQE 145
Cdd:COG2304    168 LGAGLELAYELA---RKHFIPGRVNRVILLTDGDanvGITDPEELLKLAEEAREEGITLTTLGVGSDYNE 234
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 2-152 2.62e-05

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 46.98  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMKDFVKALMgEFASTSTLFSLMQYSNILKTHFTFTEFKNILDPQSLVDpIVQLQGLTYTAT 81
Cdd:COG2425    120 PVVLCVDTSGSMAGSKEAAAKAAALALL-RALRPNRRFGVILFDTEVVEDLPLTADDGLEDAIEFLS-GLFAGGGTDIAP 197

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958649268   82 GIRTVVEELfhsknGSRKSAKKILLVITDGQKYRDPLEYSDVIpAADKAGIIRYAIGVGDAfQEPTALKEL 152
Cdd:COG2425    198 ALRAALELL-----EEPDYRNADIVLITDGEAGVSPEELLREV-RAKESGVRLFTVAIGDA-GNPGLLEAL 261
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 309-345 6.17e-05

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 40.96  E-value: 6.17e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958649268  309 FGASLCSVDVDRDGSTDLVlIGAPHYYEQtRGGQVSV 345
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLA-VGAPGEGGA-GAGAVYV 35
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 1-173 8.85e-04

Complement factors B and C2 are two critical proteases for complement activation. They both contain three CCP or Sushi domains, a trypsin-type serine protease domain and a single VWA domain with a conserved metal ion dependent adhesion site referred commonly as the MIDAS motif. Orthologues of these molecules are found from echinoderms to chordates. During complement activation, the CCP domains are cleaved off, resulting in the formation of an active protease that cleaves and activates complement C3. Complement C2 is in the classical pathway and complement B is in the alternative pathway. The interaction of C2 with C4 and of factor B with C3b are both dependent on Mg2+ binding sites within the VWA domains and the VWA domain of factor B has been shown to mediate the binding of C3. This is consistent with the common inferred function of VWA domains as magnesium-dependent protein interaction domains.


Pssm-ID: 238747 [Multi-domain]  Cd Length: 198  Bit Score: 41.50  E-value: 8.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    1 MDIAFLIDGSGSINQRDFAQMKDFVKALMGEFAS--TSTLFSLMQYSNILKthftftEFKNILDPQS--LVDPIVQLQGL 76
Cdd:cd01470      1 LNIYIALDASDSIGEEDFDEAKNAIKTLIEKISSyeVSPRYEIISYASDPK------EIVSIRDFNSndADDVIKRLEDF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   77 TY----------TATGIRTVVEELFHSKNGSRKSAKKI---LLVITDGqKYR---DPLEYSDVIPAADKAGIIR------ 134
Cdd:cd01470     75 NYddhgdktgtnTAAALKKVYERMALEKVRNKEAFNETrhvIILFTDG-KSNmggSPLPTVDKIKNLVYKNNKSdnpred 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958649268  135 ----YAIGVGDAFQEPtalkELNTIGSAPPQD-HVFKVGNFAAL 173
Cdd:cd01470    154 yldvYVFGVGDDVNKE----ELNDLASKKDNErHFFKLKDYEDL 193
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 433-457 1.21e-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: 38.13  E-value: 1.21e-03
                            10        20
                    ....*....|....*....|....*
gi 1958649268   433 QYFGQSLSGGQDLTQDGLVDLAVGA 457
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGA 27
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 4-145 1.28e-03

VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 40.72  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    4 AFLIDGSGSINQRDFAQMKDFVKALMGEFASTSTLfSLMQYSNILKThftftefknILDPQS------LVDPIVQLQ--G 75
Cdd:cd01465      4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRL-AIVTYDGAAET---------VLPATPvrdkaaILAAIDRLTagG 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958649268   76 LTYTATGIRTVVEELfhsKNGSRKSAKKILLVITDGQKY---RDPLEYSDVIPAADKAGIIRYAIGVGDAFQE 145
Cdd:cd01465     74 STAGGAGIQLGYQEA---QKHFVPGGVNRILLATDGDFNvgeTDPDELARLVAQKRESGITLSTLGFGDNYNE 143
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 974-987 1.96e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 36.32  E-value: 1.96e-03
                           10
                   ....*....|....
gi 1958649268  974 KLGFFKRQYKEMLD 987
Cdd:pfam00357    1 KCGFFKRNYPPQEE 14
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 2-141 2.24e-03

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


Pssm-ID: 238744 [Multi-domain]  Cd Length: 180  Bit Score: 40.01  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268    2 DIAFLIDGSGSINQRDFAQMK--DFVKALMGEFASTstlfslMQYSNILKTHF---TFTEFKNILDPQSLVDPIVQLQGL 76
Cdd:cd01467      4 DIMIALDVSGSMLAQDFVKPSrlEAAKEVLSDFIDR------RENDRIGLVVFagaAFTQAPLTLDRESLKELLEDIKIG 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958649268   77 -----TYTATGIRTVVEELFHSKngsrkSAKKILLVITDGQKYRDPLEYSDVIPAADKAGIIRYAIGVGD 141
Cdd:cd01467     78 lagqgTAIGDAIGLAIKRLKNSE-----AKERVIVLLTDGENNAGEIDPATAAELAKNKGVRIYTIGVGK 142
 
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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