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Conserved domains on  [gi|767988554|ref|XP_011544152|]
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integrin alpha-M isoform X1 [Homo sapiens]

Protein Classification

VWA domain-containing protein( domain architecture ID 11546373)

VWA (von Willebrand factor type A) domain-containing protein similar to mammalian alpha subunits of integrins

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 ...
 87-262 1.63e-92

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: 292.72  E-value: 1.63e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   87 SDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKK--SKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTH 164
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  165 TATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGyEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASK 244
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 767988554  245 PPRDHVFQVNNFEALKTI 262
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 ...
 554-917 1.57e-36

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: 144.39  E-value: 1.57e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   554 QPVLRVKAIMEFNPREVARNVFECNDQVVKGkeagevrVCLHVQ---KSTRDRLREGQIqsVVTYDLALDSGRPH---SR 627
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPV-------SCFTVRacfSYTGKPIPNPSL--VLNYELELDRQKKKglpPR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   628 AVFNETKNSTRRQTQVL--GLTQTCETLKLQLPNCIEDPVSPIVLRLNFSLVGTPL--SAFGNLRPVLAEDAQRLFTALF 703
Cdd:pfam08441   72 VLFLDSQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQA 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   704 PFEKNCGNDNICQDDLSITFSFMSLDC---LVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLDLSYRKVSTLQNQRSqr 780
Cdd:pfam08441  152 NFLKDCGEDNVCVPDLQLSAKFDSRESdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ-- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   781 swrLACESASSTEVSGALkstsCSINHPiFPENSEVTFNITFDV----DSKASLgnKLLLKANVTSENNMPrTNKTEfqL 856
Cdd:pfam08441  230 ---LSCTAKKENSTRQVV----CDLGNP-MKRGTQVTFGLRFSVsgleLSTEEL--SFDLQIRSTNEQNSN-SNPVS--L 296

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767988554   857 ELPVKYAVYmvVTSHGVSTK---YLNFTASENTSRV---------MQHQYQVSNLGQRSLP-ISLVFLVPVRLN 917
Cdd:pfam08441  297 KVPVVAEAQ--LSLSGVSKPdqvVGGSVKGESAMKPrseedigplVEHTYEVINNGPSTVSgASLEISWPYELS 368
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 455-501 3.46e-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: 59.31  E-value: 3.46e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 767988554    455 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNR--GAVYLFHGTSGSG 501
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGG 49
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 391-433 1.23e-08

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 51.99  E-value: 1.23e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 767988554    391 IGAYFGASLCSV-DVDSNGSTDLVlIGAPHYYEQTRGGQVSVCP 433
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYF 43
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1068-1082 2.69e-04

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


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 39.02  E-value: 2.69e-04
                           10
                   ....*....|....*
gi 767988554  1068 KLGFFKRQYKDMMSE 1082
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 ...
 87-262 1.63e-92

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: 292.72  E-value: 1.63e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   87 SDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKK--SKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTH 164
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  165 TATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGyEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASK 244
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 767988554  245 PPRDHVFQVNNFEALKTI 262
Cdd:cd01469   160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
88-265 2.51e-46

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 163.99  E-value: 2.51e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554    88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQL--KKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRT-H 164
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   165 TATGIRKVVRELFNITNGARKNAFKILVVITDGEK-FGDPlgyEDVIPEADREGVIRYVIGVGDAfrsekSRQELNTIAS 243
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDP---EEVARELKSAGVTVFAVGVGNA-----DDEELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 767988554   244 KPPRDHVFQVNNFEALKTIQNQ 265
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 88-259 1.07e-39

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: 144.90  E-value: 1.07e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554     88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKS--KTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLL-GRTH 164
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554    165 TATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFrsekSRQELNTIASK 244
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV----DEEELKKLASA 156

                           170
                    ....*....|....*
gi 767988554    245 PPRDHVFQVNNFEAL 259
Cdd:smart00327  157 PGGVYVFLPELLDLL 171
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 554-917 1.57e-36

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: 144.39  E-value: 1.57e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   554 QPVLRVKAIMEFNPREVARNVFECNDQVVKGkeagevrVCLHVQ---KSTRDRLREGQIqsVVTYDLALDSGRPH---SR 627
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPV-------SCFTVRacfSYTGKPIPNPSL--VLNYELELDRQKKKglpPR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   628 AVFNETKNSTRRQTQVL--GLTQTCETLKLQLPNCIEDPVSPIVLRLNFSLVGTPL--SAFGNLRPVLAEDAQRLFTALF 703
Cdd:pfam08441   72 VLFLDSQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQA 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   704 PFEKNCGNDNICQDDLSITFSFMSLDC---LVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLDLSYRKVSTLQNQRSqr 780
Cdd:pfam08441  152 NFLKDCGEDNVCVPDLQLSAKFDSRESdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ-- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   781 swrLACESASSTEVSGALkstsCSINHPiFPENSEVTFNITFDV----DSKASLgnKLLLKANVTSENNMPrTNKTEfqL 856
Cdd:pfam08441  230 ---LSCTAKKENSTRQVV----CDLGNP-MKRGTQVTFGLRFSVsgleLSTEEL--SFDLQIRSTNEQNSN-SNPVS--L 296

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767988554   857 ELPVKYAVYmvVTSHGVSTK---YLNFTASENTSRV---------MQHQYQVSNLGQRSLP-ISLVFLVPVRLN 917
Cdd:pfam08441  297 KVPVVAEAQ--LSLSGVSKPdqvVGGSVKGESAMKPrseedigplVEHTYEVINNGPSTVSgASLEISWPYELS 368
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 455-501 3.46e-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: 59.31  E-value: 3.46e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 767988554    455 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNR--GAVYLFHGTSGSG 501
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGG 49
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 391-433 1.23e-08

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 51.99  E-value: 1.23e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 767988554    391 IGAYFGASLCSV-DVDSNGSTDLVlIGAPHYYEQTRGGQVSVCP 433
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYF 43
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 83-242 1.14e-07

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: 54.17  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   83 PQEDSDIAFLIDGSGSIIPHD-FRRMKEFVSTVMEQLKKsKTLFSLMQYSEEFRIH--FTFkefqnnpNPRSLVKPITQL 159
Cdd:COG1240    89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP-RDRVGLVAFGGEAEVLlpLTR-------DREALKRALDEL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  160 --LGRTHTATGIRKVVRELfnitNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAfrsEKSRQE 237
Cdd:COG1240   161 ppGGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE---AVDEGL 233


                  ....*
gi 767988554  238 LNTIA 242
Cdd:COG1240   234 LREIA 238
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 459-494 1.96e-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: 48.28  E-value: 1.96e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 767988554   459 FGAALTVlGDVNGDKLTDVAIGAPGE-EDNRGAVYLF 494
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1068-1082 2.69e-04

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 39.02  E-value: 2.69e-04
                           10
                   ....*....|....*
gi 767988554  1068 KLGFFKRQYKDMMSE 1082
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 395-431 4.43e-04

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 38.65  E-value: 4.43e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 767988554   395 FGASLCSVDVDSNGSTDLVlIGAPHYYEQtRGGQVSV 431
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLA-VGAPGEGGA-GAGAVYV 35
 
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 ...
 87-262 1.63e-92

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: 292.72  E-value: 1.63e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   87 SDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKK--SKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTH 164
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  165 TATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGyEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASK 244
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 767988554  245 PPRDHVFQVNNFEALKTI 262
Cdd:cd01469   160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
88-265 2.51e-46

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 163.99  E-value: 2.51e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554    88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQL--KKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRT-H 164
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   165 TATGIRKVVRELFNITNGARKNAFKILVVITDGEK-FGDPlgyEDVIPEADREGVIRYVIGVGDAfrsekSRQELNTIAS 243
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDP---EEVARELKSAGVTVFAVGVGNA-----DDEELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 767988554   244 KPPRDHVFQVNNFEALKTIQNQ 265
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 88-259 1.07e-39

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: 144.90  E-value: 1.07e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554     88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKS--KTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLL-GRTH 164
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554    165 TATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFrsekSRQELNTIASK 244
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV----DEEELKKLASA 156

                           170
                    ....*....|....*
gi 767988554    245 PPRDHVFQVNNFEAL 259
Cdd:smart00327  157 PGGVYVFLPELLDLL 171
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 554-917 1.57e-36

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: 144.39  E-value: 1.57e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   554 QPVLRVKAIMEFNPREVARNVFECNDQVVKGkeagevrVCLHVQ---KSTRDRLREGQIqsVVTYDLALDSGRPH---SR 627
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPV-------SCFTVRacfSYTGKPIPNPSL--VLNYELELDRQKKKglpPR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   628 AVFNETKNSTRRQTQVL--GLTQTCETLKLQLPNCIEDPVSPIVLRLNFSLVGTPL--SAFGNLRPVLAEDAQRLFTALF 703
Cdd:pfam08441   72 VLFLDSQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQA 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   704 PFEKNCGNDNICQDDLSITFSFMSLDC---LVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLDLSYRKVSTLQNQRSqr 780
Cdd:pfam08441  152 NFLKDCGEDNVCVPDLQLSAKFDSRESdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ-- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   781 swrLACESASSTEVSGALkstsCSINHPiFPENSEVTFNITFDV----DSKASLgnKLLLKANVTSENNMPrTNKTEfqL 856
Cdd:pfam08441  230 ---LSCTAKKENSTRQVV----CDLGNP-MKRGTQVTFGLRFSVsgleLSTEEL--SFDLQIRSTNEQNSN-SNPVS--L 296

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767988554   857 ELPVKYAVYmvVTSHGVSTK---YLNFTASENTSRV---------MQHQYQVSNLGQRSLP-ISLVFLVPVRLN 917
Cdd:pfam08441  297 KVPVVAEAQ--LSLSGVSKPdqvVGGSVKGESAMKPrseedigplVEHTYEVINNGPSTVSgASLEISWPYELS 368
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 88-251 2.00e-34

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: 129.33  E-value: 2.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKS--KTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGR-TH 164
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGpdKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  165 TATGIRKVVRELFNITNgARKNAFKILVVITDGEKFGDPlGYEDVIPEADREGVIRYVIGVGDAfrsekSRQELNTIASK 244
Cdd:cd01450    82 TGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDGG-DPKEAAAKLKDEGIKVFVVGVGPA-----DEEELREIASC 154


                  ....*..
gi 767988554  245 PPRDHVF 251
Cdd:cd01450   155 PSERHVF 161
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 88-251 6.34e-27

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: 108.04  E-value: 6.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKS--KTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPIT-QLLGRTH 164
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASppGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  165 TATGIRKVVRELFNITNGARKnafKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDafrsEKSRQELNTIASK 244
Cdd:cd00198    82 IGAALRLALELLKSAKRPNAR---RVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGD----DANEDELKEIADK 154


                  ....*..
gi 767988554  245 PPRDHVF 251
Cdd:cd00198   155 TTGGAVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 88-256 1.83e-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: 103.91  E-value: 1.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLK--KSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHT 165
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEigPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  166 ATGIRKVVRELFNITNGARKNAFKILVVITDGeKFGDplgyeDVIPEADR---EGVIRYVIGVGDAFRSeksrqELNTIA 242
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDG-KSQD-----DVELPARVlrnLGVNVFAVGVKDADES-----ELKMIA 150

                         170
                  ....*....|....
gi 767988554  243 SKPPRDHVFQVNNF 256
Cdd:cd01482   151 SKPSETHVFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 88-256 5.21e-25

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: 102.31  E-value: 5.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKS--KTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHT 165
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGpdGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  166 ATGIRKVVRELFNITNGARKNAFKILVVITDGEKfgdplgYEDVIPEAD---REGVIRYVIGVGDAfrsekSRQELNTIA 242
Cdd:cd01472    82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKS------QDDVEEPAVelkQAGIEVFAVGVKNA-----DEEELKQIA 150

                         170
                  ....*....|....
gi 767988554  243 SKPPRDHVFQVNNF 256
Cdd:cd01472   151 SDPKELYVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 88-270 8.68e-22

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 95.14  E-value: 8.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSK--TLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHT 165
Cdd:cd01475     4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPdaTRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  166 ATGIRKVVRELFNITNGARK---NAFKILVVITDGEKfGDPLGyeDVIPEADREGVIRYVIGVGDAFRSeksrqELNTIA 242
Cdd:cd01475    84 GLAIQYAMNNAFSEAEGARPgseRVPRVGIVVTDGRP-QDDVS--EVAAKARALGIEMFAVGVGRADEE-----ELREIA 155

                         170       180
                  ....*....|....*....|....*...
gi 767988554  243 SKPPRDHVFQVNNFEALKTIQNQLREKI 270
Cdd:cd01475   156 SEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 88-269 5.81e-15

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: 74.47  E-value: 5.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   88 DIAFLIDGSGSIIpHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHTAT 167
Cdd:cd01474     6 DLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  168 GIRKVVRELFNITNGARKNAfKILVVITDGEKFGDPLGY-EDVIPEADREGVIRYVIGVGDAfrsekSRQELNTIASKPp 246
Cdd:cd01474    85 GLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKYpEHEAKLSRKLGAIVYCVGVTDF-----LKSQLINIADSK- 157

                         170       180
                  ....*....|....*....|....
gi 767988554  247 rDHVFQVNN-FEALKTIQNQLREK 269
Cdd:cd01474   158 -EYVFPVTSgFQALSGIIESVVKK 180
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 87-251 6.39e-13

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: 67.81  E-value: 6.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   87 SDIAFLIDGSGSIIpHDFRRMKEFVSTVMEQLK--KSKTLFSLMQYSEEFR--IHFTFKEFQNNPNPRSLVKPITQLLGR 162
Cdd:cd01476     1 LDLLFVLDSSGSVR-GKFEKYKKYIERIVEGLEigPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  163 THTATGIRKVVrELFNITNGARKNAFKILVVITDGEKFGDPLGyedvIPEADREGVIRYVIGVGDAFRSEKSRQELNTIA 242
Cdd:cd01476    80 TATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEK----QARILRAVPNIETFAVGTGDPGTVDTEELHSIT 154


                  ....*....
gi 767988554  243 SKPprDHVF 251
Cdd:cd01476   155 GNE--DHIF 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 88-256 5.94e-12

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: 65.04  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLK--KSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPItQLLGRTHT 165
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTHSTKADVLGAVRRL-RLRGGSQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  166 ATG--IRKVVRELFNITNGAR--KNAFKILVVITDGEKFGDplgYEDVIPEADREGVIRYVIGVGDAfrsekSRQELNTI 241
Cdd:cd01481    81 NTGsaLDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDD---VERPAVALKRAGIVPFAIGARNA-----DLAELQQI 152

                         170
                  ....*....|....*
gi 767988554  242 ASKPprDHVFQVNNF 256
Cdd:cd01481   153 AFDP--SFVFQVSDF 165
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 455-501 3.46e-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: 59.31  E-value: 3.46e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 767988554    455 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNR--GAVYLFHGTSGSG 501
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSGGG 49
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 88-235 9.11e-11

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: 62.02  E-value: 9.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   88 DIAFLIDGSGSI-IPHDFRRMKEFVSTVMEQLKKSK--TLFSLMQYSEEFRIHFTFKEFqNNPNPRSLVKPITQLL---- 160
Cdd:cd01471     2 DLYLLVDGSGSIgYSNWVTHVVPFLHTFVQNLNISPdeINLYLVTFSTNAKELIRLSSP-NSTNKDLALNAIRALLslyy 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767988554  161 --GRTHTATGIrKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADReGVIRYVIGVGDAFRSEKSR 235
Cdd:cd01471    81 pnGSTNTTSAL-LVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTLKEARKLRER-GVIIAVLGVGQGVNHEENR 155
VWA_2 pfam13519
von Willebrand factor type A domain;
89-194 7.97e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 56.92  E-value: 7.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554    89 IAFLIDGSGSI-----IPHDFRRMKEFVSTVMEQLKKSKtlFSLMQYSEEFRIHFTFKefQNNPNPRSLVKPITQLLGRT 163
Cdd:pfam13519    1 LVFVLDTSGSMrngdyGPTRLEAAKDAVLALLKSLPGDR--VGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGGGT 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 767988554   164 HTATGIRKVVRELFNITNGARknafKILVVI 194
Cdd:pfam13519   77 NLAAALQLARAALKHRRKNQP----RRIVLI 103
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 88-259 1.08e-09

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 58.94  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTL--------FSLMQYSEEFRIHFTFKEFQNNPNP-RSLVKPITQ 158
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagswrVGVVQYSDQQEVEAGFLRDIRNYTSlKEAVDNLEY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  159 LLGRTHTATGIRKVVRELFNITNGARKnafKILVVITDGEKFG-DPLGYEDVIPEADREGVIRYVIGVGdAFRSEKsrqe 237
Cdd:cd01480    84 IGGGTFTDCALKYATEQLLEGSHQKEN---KFLLVITDGHSDGsPDGGIEKAVNEADHLGIKIFFVAVG-SQNEEP---- 155

                         170       180
                  ....*....|....*....|..
gi 767988554  238 LNTIASKPPRDHvfQVNNFEAL 259
Cdd:cd01480   156 LSRIACDGKSAL--YRENFAEL 175
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 391-433 1.23e-08

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 51.99  E-value: 1.23e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 767988554    391 IGAYFGASLCSV-DVDSNGSTDLVlIGAPHYYEQTRGGQVSVCP 433
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYF 43
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 83-242 1.14e-07

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: 54.17  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   83 PQEDSDIAFLIDGSGSIIPHD-FRRMKEFVSTVMEQLKKsKTLFSLMQYSEEFRIH--FTFkefqnnpNPRSLVKPITQL 159
Cdd:COG1240    89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP-RDRVGLVAFGGEAEVLlpLTR-------DREALKRALDEL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  160 --LGRTHTATGIRKVVRELfnitNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAfrsEKSRQE 237
Cdd:COG1240   161 ppGGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE---AVDEGL 233


                  ....*
gi 767988554  238 LNTIA 242
Cdd:COG1240   234 LREIA 238
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 459-494 1.96e-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: 48.28  E-value: 1.96e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 767988554   459 FGAALTVlGDVNGDKLTDVAIGAPGE-EDNRGAVYLF 494
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
vWA_complement_factors cd01470
Complement factors B and C2 are two critical proteases for complement activation. They both ...
 88-260 3.30e-05

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: 46.13  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   88 DIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLK--KSKTLFSLMQYSEEFRIHFTFKEFQNNpNPRSLVKPITQLLGRTH- 164
Cdd:cd01470     2 NIYIALDASDSIGEEDFDEAKNAIKTLIEKISsyEVSPRYEIISYASDPKEIVSIRDFNSN-DADDVIKRLEDFNYDDHg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  165 --TATGIR---KVVRELFNITNGARKNAFK----ILVVITDGeKF---GDPLGYEDVI---------PEADREGVIR-YV 222
Cdd:cd01470    81 dkTGTNTAaalKKVYERMALEKVRNKEAFNetrhVIILFTDG-KSnmgGSPLPTVDKIknlvyknnkSDNPREDYLDvYV 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767988554  223 IGVGDAFRSEksrqELNTIASKPPRD-HVFQVNNFEALK 260
Cdd:cd01470   160 FGVGDDVNKE----ELNDLASKKDNErHFFKLKDYEDLQ 194
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 87-244 1.04e-04

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 45.48  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   87 SDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLkKSKTLFSLMQYSEEFRihfTFKEFQNNPNPRSLVKPITQLL--GRTH 164
Cdd:COG2304    92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL-RPGDRVSIVTFAGDAR---VLLPPTPATDRAKILAAIDRLQagGGTA 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  165 TATGIRKVVRELfniTNGARKNAFKILVVITDGE---KFGDPLGYEDVIPEADREGVIRYVIGVGDAFRseksRQELNTI 241
Cdd:COG2304   168 LGAGLELAYELA---RKHFIPGRVNRVILLTDGDanvGITDPEELLKLAEEAREEGITLTTLGVGSDYN----EDLLERL 240


                  ...
gi 767988554  242 ASK 244
Cdd:COG2304   241 ADA 243
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1068-1082 2.69e-04

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 39.02  E-value: 2.69e-04
                           10
                   ....*....|....*
gi 767988554  1068 KLGFFKRQYKDMMSE 1082
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 395-431 4.43e-04

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 38.65  E-value: 4.43e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 767988554   395 FGASLCSVDVDSNGSTDLVlIGAPHYYEQtRGGQVSV 431
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLA-VGAPGEGGA-GAGAVYV 35
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 63-228 1.53e-03

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 41.59  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   63 LFGSNLRQQPQKFPEALRGCPQEDSDIAFLIDGSGSiiphdfrrM--------KEFVSTVMEQLKKSKTlFSLMQYSEEF 134
Cdd:COG2425    95 LALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGS--------MagskeaaaKAAALALLRALRPNRR-FGVILFDTEV 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  135 RIHFTFKefqNNPNPRSLVKPI--TQLLGRTHTATGIRKVVRELfnitnGARKNAFKILVVITDGEkfgDPLGYEDVIPE 212
Cdd:COG2425   166 VEDLPLT---ADDGLEDAIEFLsgLFAGGGTDIAPALRAALELL-----EEPDYRNADIVLITDGE---AGVSPEELLRE 234

                         170
                  ....*....|....*...
gi 767988554  213 AD-REGVIR-YVIGVGDA 228
Cdd:COG2425   235 VRaKESGVRlFTVAIGDA 252
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 89-234 2.01e-03

norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.


Pssm-ID: 238731 [Multi-domain]  Cd Length: 174  Bit Score: 40.39  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554   89 IAFLIDGSGSIipHDFRRMKEFVSTVM---EQLKKSKTLFSLMQYS------EEFRIhFTFKEFQNNPNPRSLvKPITQL 159
Cdd:cd01454     3 VTLLLDLSGSM--RSDRRIDVAKKAAVllaEALEACGVPHAILGFTtdaggrERVRW-IKIKDFDESLHERAR-KRLAAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988554  160 LGRTHTATG--IRKVVRELfnitnGARKNAFKILVVITDGEKF------GDPLGYED---VIPEADREGVIRYVIGVG-D 227
Cdd:cd01454    79 SPGGNTRDGaaIRHAAERL-----LARPEKRKILLVISDGEPNdldyyeGNVFATEDalrAVIEARKLGIEVFGITIDrD 153


                  ....*..
gi 767988554  228 AFRSEKS 234
Cdd:cd01454   154 ATTVDKE 160
 
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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