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Conserved domains on  [gi|132626289|ref|NP_001076429|]
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integrin alpha-M isoform 1 precursor [Mus musculus]

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 ...
 149-324 4.43e-84

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: 270.77  E-value: 4.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  149 SDIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKK--SKTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGRTK 226
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  227 TASGIRKVVRELFHKTNGARENAAKILVVITDGEKFGDPLDyKDVIPEADRAGVIRYVIGVGNAFNKPQSRRELDTIASK 306
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 132626289  307 PAGEHVFQVDNFEALNTI 324
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 ...
 616-1034 1.43e-30

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


The actual alignment was detected with superfamily member pfam08441:

Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 126.67  E-value: 1.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   616 QPVLRLEATMEFSPKKVARSVFACQEQVLKNKdAGEVRVCLRVRKNTKDRlreGDIqsTVTYDLALD----PGRSRiRAF 691
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS-CFTVRACFSYTGKPIPN---PSL--VLNYELELDrqkkKGLPP-RVL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   692 FDETK--NNTRRRTQVFGLMQKCETLKLILPDCVDDSVSPIILRLNYTLVGEPL--RSFGNLRPVLAMDAQRFFTAMFPF 767
Cdd:pfam08441   74 FLDSQqpSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANF 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   768 EKNCGNDSICQDDLSitMSAMGLDT-----LVVGGPQDFNMSVTLRNDGEDSYGTQVTVYYPSGLSYRKdsasqnpltkk 842
Cdd:pfam08441  154 LKDCGEDNVCVPDLQ--LSAKFDSResdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSG----------- 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   843 pwfVKPAESSSSSEGHGALKSTTWNINHPI---FPANSEVTFNVTFDV----DSHASFgnKLLLKAIVASENNMsrtHKT 915
Cdd:pfam08441  221 ---VRREGSEKQLSCTAKKENSTRQVVCDLgnpMKRGTQVTFGLRFSVsgleLSTEEL--SFDLQIRSTNEQNS---NSN 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   916 KFQLELPVKYAIYMIVT--SD-----------ESSIRYlnFTASEMTSKViQHQYQFNNLGQRSLPVSV--VFWiPVQIN 980
Cdd:pfam08441  293 PVSLKVPVVAEAQLSLSgvSKpdqvvggsvkgESAMKP--RSEEDIGPLV-EHTYEVINNGPSTVSGASleISW-PYELS 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   981 N---------VTVWD----HPQ-VIFSQNLSSACHTEQKSPPHSNFRDQLERTP------------VLNCSVAV-CKRIQ 1033
Cdd:pfam08441  369 NgkwllylldVQGQGkgecSPQnEINPLNLTQSLESSKPLRTSRVHHVVKRRDVlksekatqtasvLLSCDSGArCVVIR 448


                   .
gi 132626289  1034 C 1034
Cdd:pfam08441  449 C 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-558 1.13e-10

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: 58.16  E-value: 1.13e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 132626289    517 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEQENQ--GAVYIFYG 558
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG 44
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 453-495 6.35e-07

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 47.37  E-value: 6.35e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 132626289    453 IGSYFGASLCSV-DMDADGNTNLiLIGAPHYYEKTRGGQVSVCP 495
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDL-LVGAPRANDAGETGAVYVYF 43
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 582-620 5.41e-04

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 39.28  E-value: 5.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 132626289    582 QYFGQSLSGGKDLTMDGLMDLAVGA--QGHLLLLRAQPVLR 620
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprANDAGETGAVYVYF 43
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1131-1143 1.15e-03

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


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 37.09  E-value: 1.15e-03
                           10
                   ....*....|...
gi 132626289  1131 KLGFFKRQYKDMM 1143
Cdd:pfam00357    1 KCGFFKRNYPPQE 13
 
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 ...
 149-324 4.43e-84

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: 270.77  E-value: 4.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  149 SDIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKK--SKTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGRTK 226
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  227 TASGIRKVVRELFHKTNGARENAAKILVVITDGEKFGDPLDyKDVIPEADRAGVIRYVIGVGNAFNKPQSRRELDTIASK 306
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 132626289  307 PAGEHVFQVDNFEALNTI 324
Cdd:cd01469   160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
150-327 2.36e-52

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 181.32  E-value: 2.36e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQF--KKSKTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGRTK- 226
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   227 TASGIRKVVRELFHKTNGARENAAKILVVITDGEKFGDplDYKDVIPEADRAGVIRYVIGVGNAFNKpqsrrELDTIASK 306
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVGNADDE-----ELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 132626289   307 PAGEHVFQVDNFEALNTIQNQ 327
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 150-325 3.57e-45

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: 160.70  E-value: 3.57e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289    150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKKS--KTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIK-QLNGRTK 226
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289    227 TASGIRKVVRELFHKTNGARENAAKILVVITDGEKFGDPLDYKDVIPEADRAGVIRYVIGVGNAFNKPqsrrELDTIASK 306
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEE----ELKKLASA 156

                           170
                    ....*....|....*....
gi 132626289    307 PAGEHVFQVDNFEALNTIQ 325
Cdd:smart00327  157 PGGVYVFLPELLDLLIDLL 175
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 616-1034 1.43e-30

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 126.67  E-value: 1.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   616 QPVLRLEATMEFSPKKVARSVFACQEQVLKNKdAGEVRVCLRVRKNTKDRlreGDIqsTVTYDLALD----PGRSRiRAF 691
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS-CFTVRACFSYTGKPIPN---PSL--VLNYELELDrqkkKGLPP-RVL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   692 FDETK--NNTRRRTQVFGLMQKCETLKLILPDCVDDSVSPIILRLNYTLVGEPL--RSFGNLRPVLAMDAQRFFTAMFPF 767
Cdd:pfam08441   74 FLDSQqpSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANF 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   768 EKNCGNDSICQDDLSitMSAMGLDT-----LVVGGPQDFNMSVTLRNDGEDSYGTQVTVYYPSGLSYRKdsasqnpltkk 842
Cdd:pfam08441  154 LKDCGEDNVCVPDLQ--LSAKFDSResdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSG----------- 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   843 pwfVKPAESSSSSEGHGALKSTTWNINHPI---FPANSEVTFNVTFDV----DSHASFgnKLLLKAIVASENNMsrtHKT 915
Cdd:pfam08441  221 ---VRREGSEKQLSCTAKKENSTRQVVCDLgnpMKRGTQVTFGLRFSVsgleLSTEEL--SFDLQIRSTNEQNS---NSN 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   916 KFQLELPVKYAIYMIVT--SD-----------ESSIRYlnFTASEMTSKViQHQYQFNNLGQRSLPVSV--VFWiPVQIN 980
Cdd:pfam08441  293 PVSLKVPVVAEAQLSLSgvSKpdqvvggsvkgESAMKP--RSEEDIGPLV-EHTYEVINNGPSTVSGASleISW-PYELS 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   981 N---------VTVWD----HPQ-VIFSQNLSSACHTEQKSPPHSNFRDQLERTP------------VLNCSVAV-CKRIQ 1033
Cdd:pfam08441  369 NgkwllylldVQGQGkgecSPQnEINPLNLTQSLESSKPLRTSRVHHVVKRRDVlksekatqtasvLLSCDSGArCVVIR 448


                   .
gi 132626289  1034 C 1034
Cdd:pfam08441  449 C 449
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 145-328 1.56e-12

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: 69.20  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  145 PQQESDIVFLIDGSGSINNID-FQKMKEFVSTVMEQFKKsKTLFSLMQYSDEFRIHFtfndfkrnPSPRSHVSPIKQLN- 222
Cdd:COG1240    89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP-RDRVGLVAFGGEAEVLL--------PLTRDREALKRALDe 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  223 ----GRTKTASGIRKVVRELfhktNGARENAAKILVVITDGEKFGDPLDYKDVIPEADRAGVIRYVIGVGNAfnkPQSRR 298
Cdd:COG1240   160 lppgGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE---AVDEG 232

                         170       180       190
                  ....*....|....*....|....*....|
gi 132626289  299 ELDTIASKPAGEHvFQVDNFEALNTIQNQL 328
Cdd:COG1240   233 LLREIAEATGGRY-FRADDLSELAAIYREI 261
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-558 1.13e-10

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: 58.16  E-value: 1.13e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 132626289    517 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEQENQ--GAVYIFYG 558
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG 44
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 521-556 3.59e-08

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 50.20  E-value: 3.59e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 132626289   521 FGAALTVlGDVNGDKLTDVAIGAPGE-QENQGAVYIF 556
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 453-495 6.35e-07

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 47.37  E-value: 6.35e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 132626289    453 IGSYFGASLCSV-DMDADGNTNLiLIGAPHYYEKTRGGQVSVCP 495
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDL-LVGAPRANDAGETGAVYVYF 43
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 582-620 5.41e-04

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 39.28  E-value: 5.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 132626289    582 QYFGQSLSGGKDLTMDGLMDLAVGA--QGHLLLLRAQPVLR 620
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprANDAGETGAVYVYF 43
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1131-1143 1.15e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 37.09  E-value: 1.15e-03
                           10
                   ....*....|...
gi 132626289  1131 KLGFFKRQYKDMM 1143
Cdd:pfam00357    1 KCGFFKRNYPPQE 13
 
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 ...
 149-324 4.43e-84

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: 270.77  E-value: 4.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  149 SDIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKK--SKTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGRTK 226
Cdd:cd01469     1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  227 TASGIRKVVRELFHKTNGARENAAKILVVITDGEKFGDPLDyKDVIPEADRAGVIRYVIGVGNAFNKPQSRRELDTIASK 306
Cdd:cd01469    81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                         170
                  ....*....|....*...
gi 132626289  307 PAGEHVFQVDNFEALNTI 324
Cdd:cd01469   160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
150-327 2.36e-52

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 181.32  E-value: 2.36e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQF--KKSKTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGRTK- 226
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTTn 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   227 TASGIRKVVRELFHKTNGARENAAKILVVITDGEKFGDplDYKDVIPEADRAGVIRYVIGVGNAFNKpqsrrELDTIASK 306
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSQDG--DPEEVARELKSAGVTVFAVGVGNADDE-----ELRKIASE 153

                          170       180
                   ....*....|....*....|.
gi 132626289   307 PAGEHVFQVDNFEALNTIQNQ 327
Cdd:pfam00092  154 PGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 150-325 3.57e-45

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: 160.70  E-value: 3.57e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289    150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKKS--KTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIK-QLNGRTK 226
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289    227 TASGIRKVVRELFHKTNGARENAAKILVVITDGEKFGDPLDYKDVIPEADRAGVIRYVIGVGNAFNKPqsrrELDTIASK 306
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDVDEE----ELKKLASA 156

                           170
                    ....*....|....*....
gi 132626289    307 PAGEHVFQVDNFEALNTIQ 325
Cdd:smart00327  157 PGGVYVFLPELLDLLIDLL 175
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 150-313 5.70e-36

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: 133.96  E-value: 5.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKKS--KTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGR-TK 226
Cdd:cd01450     2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGpdKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  227 TASGIRKVVRELFHKTNgARENAAKILVVITDGEKFGDPlDYKDVIPEADRAGVIRYVIGVGNAFNKpqsrrELDTIASK 306
Cdd:cd01450    82 TGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDGG-DPKEAAAKLKDEGIKVFVVGVGPADEE-----ELREIASC 154


                  ....*..
gi 132626289  307 PAGEHVF 313
Cdd:cd01450   155 PSERHVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 150-318 5.52e-32

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: 122.40  E-value: 5.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQFK--KSKTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGRTKT 227
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEigPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  228 ASGIRKVVRELFHKTNGARENAAKILVVITDGeKFGDplDYKDVIPEADRAGVIRYVIGVGNAfnkpqSRRELDTIASKP 307
Cdd:cd01482    82 GKALTHVREKNFTPDAGARPGVPKVVILITDG-KSQD--DVELPARVLRNLGVNVFAVGVKDA-----DESELKMIASKP 153

                         170
                  ....*....|.
gi 132626289  308 AGEHVFQVDNF 318
Cdd:cd01482   154 SETHVFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 150-318 7.39e-31

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: 119.25  E-value: 7.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKKS--KTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGRTKT 227
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGpdGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  228 ASGIRKVVRELFHKTNGARENAAKILVVITDGEkfgdPLDykDVIPEAD---RAGVIRYVIGVGNAFNKpqsrrELDTIA 304
Cdd:cd01472    82 GKALKYVRENLFTEASGSREGVPKVLVVITDGK----SQD--DVEEPAVelkQAGIEVFAVGVKNADEE-----ELKQIA 150

                         170
                  ....*....|....
gi 132626289  305 SKPAGEHVFQVDNF 318
Cdd:cd01472   151 SDPKELYVFNVADF 164
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 616-1034 1.43e-30

Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C terminus of a number of pfam01839 repeats and to the N-terminus of the pfam00357 cytoplasmic region. This region is composed of three immunoglobulin-like domains.


Pssm-ID: 462478 [Multi-domain]  Cd Length: 449  Bit Score: 126.67  E-value: 1.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   616 QPVLRLEATMEFSPKKVARSVFACQEQVLKNKdAGEVRVCLRVRKNTKDRlreGDIqsTVTYDLALD----PGRSRiRAF 691
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS-CFTVRACFSYTGKPIPN---PSL--VLNYELELDrqkkKGLPP-RVL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   692 FDETK--NNTRRRTQVFGLMQKCETLKLILPDCVDDSVSPIILRLNYTLVGEPL--RSFGNLRPVLAMDAQRFFTAMFPF 767
Cdd:pfam08441   74 FLDSQqpSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANF 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   768 EKNCGNDSICQDDLSitMSAMGLDT-----LVVGGPQDFNMSVTLRNDGEDSYGTQVTVYYPSGLSYRKdsasqnpltkk 842
Cdd:pfam08441  154 LKDCGEDNVCVPDLQ--LSAKFDSResdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSG----------- 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   843 pwfVKPAESSSSSEGHGALKSTTWNINHPI---FPANSEVTFNVTFDV----DSHASFgnKLLLKAIVASENNMsrtHKT 915
Cdd:pfam08441  221 ---VRREGSEKQLSCTAKKENSTRQVVCDLgnpMKRGTQVTFGLRFSVsgleLSTEEL--SFDLQIRSTNEQNS---NSN 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   916 KFQLELPVKYAIYMIVT--SD-----------ESSIRYlnFTASEMTSKViQHQYQFNNLGQRSLPVSV--VFWiPVQIN 980
Cdd:pfam08441  293 PVSLKVPVVAEAQLSLSgvSKpdqvvggsvkgESAMKP--RSEEDIGPLV-EHTYEVINNGPSTVSGASleISW-PYELS 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   981 N---------VTVWD----HPQ-VIFSQNLSSACHTEQKSPPHSNFRDQLERTP------------VLNCSVAV-CKRIQ 1033
Cdd:pfam08441  369 NgkwllylldVQGQGkgecSPQnEINPLNLTQSLESSKPLRTSRVHHVVKRRDVlksekatqtasvLLSCDSGArCVVIR 448


                   .
gi 132626289  1034 C 1034
Cdd:pfam08441  449 C 449
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 150-332 6.62e-27

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: 110.17  E-value: 6.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKKSK--TLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGRTKT 227
Cdd:cd01475     4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPdaTRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  228 ASGIRKVVRELFHKTNGAR---ENAAKILVVITDGEkfgdPLDY-KDVIPEADRAGVIRYVIGVGNAfnkpqSRRELDTI 303
Cdd:cd01475    84 GLAIQYAMNNAFSEAEGARpgsERVPRVGIVVTDGR----PQDDvSEVAAKARALGIEMFAVGVGRA-----DEEELREI 154

                         170       180
                  ....*....|....*....|....*....
gi 132626289  304 ASKPAGEHVFQVDNFEALNTIQNQLQEKI 332
Cdd:cd01475   155 ASEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 150-313 7.00e-26

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: 104.96  E-value: 7.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKKS--KTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIK-QLNGRTK 226
Cdd:cd00198     2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASppGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  227 TASGIRKVVRELFhktNGARENAAKILVVITDGEKFGDPLDYKDVIPEADRAGVIRYVIGVGNAFNkpqsRRELDTIASK 306
Cdd:cd00198    82 IGAALRLALELLK---SAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGDDAN----EDELKEIADK 154


                  ....*..
gi 132626289  307 PAGEHVF 313
Cdd:cd00198   155 TTGGAVF 161
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 150-318 1.47e-16

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: 78.52  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQFK--KSKTLFSLMQYSDEFRIHFTFNDFkrnPSPRSHVSPIKQLNGRT-- 225
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTH---STKADVLGAVRRLRLRGgs 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  226 --KTASGIRKVVRELFHKTNGAR--ENAAKILVVITDGEKFGDPLDYKDVIpeaDRAGVIRYVIGVGNAfnkpqSRRELD 301
Cdd:cd01481    79 qlNTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDDVERPAVAL---KRAGIVPFAIGARNA-----DLAELQ 150

                         170
                  ....*....|....*..
gi 132626289  302 TIASKPagEHVFQVDNF 318
Cdd:cd01481   151 QIAFDP--SFVFQVSDF 165
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 149-313 1.34e-15

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: 75.51  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  149 SDIVFLIDGSGSINNIdFQKMKEFVSTVMEQFK--KSKTLFSLMQYSDEFR--IHFTFNDFKRNPSPRSHVSPIKQLNGR 224
Cdd:cd01476     1 LDLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEigPTATRVALITYSGRGRqrVRFNLPKHNDGEELLEKVDNLRFIGGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  225 TKTASGIRKVVrELFHKTNGARENAAKILVVITDGEKFGDPLDykdvIPEADRAGVIRYVIGVGNAFNKPQSRRELDTIA 304
Cdd:cd01476    80 TATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEK----QARILRAVPNIETFAVGTGDPGTVDTEELHSIT 154


                  ....*....
gi 132626289  305 SkpAGEHVF 313
Cdd:cd01476   155 G--NEDHIF 161
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 150-331 7.94e-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: 74.08  E-value: 7.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  150 DIVFLIDGSGSINNiDFQKMKEFVSTVMEQFKKSKTLFSLMQYSDEFRIHFTFNDFKRNPS----PRSHVSPikqlNGRT 225
Cdd:cd01474     6 DLYFVLDKSGSVAA-NWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIkgleVLKKVTP----SGQT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  226 KTASGIRKVVRELFHKTNGAREnAAKILVVITDGEKFGDPldYKDVIPEADRA---GVIRYVIGVgNAFNKPQsrreLDT 302
Cdd:cd01474    81 YIHEGLENANEQIFNRNGGGRE-TVSVIIALTDGQLLLNG--HKYPEHEAKLSrklGAIVYCVGV-TDFLKSQ----LIN 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 132626289  303 IASKPagEHVFQVDN-FEALNTIQNQLQEK 331
Cdd:cd01474   153 IADSK--EYVFPVTSgFQALSGIIESVVKK 180
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 150-298 9.47e-15

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: 73.57  E-value: 9.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  150 DIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKKSKTL--------FSLMQYSDEFRIHFTFNDFKRN-PSPRSHVSPIKQ 220
Cdd:cd01480     4 DITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagswrVGVVQYSDQQEVEAGFLRDIRNyTSLKEAVDNLEY 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 132626289  221 LNGRTKTASGIRKVVRELFHktnGARENAAKILVVITDGEKFGDPLD-YKDVIPEADRAGVIRYVIGVGnAFNKPQSRR 298
Cdd:cd01480    84 IGGGTFTDCALKYATEQLLE---GSHQKENKFLLVITDGHSDGSPDGgIEKAVNEADHLGIKIFFVAVG-SQNEEPLSR 158
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 145-328 1.56e-12

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: 69.20  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  145 PQQESDIVFLIDGSGSINNID-FQKMKEFVSTVMEQFKKsKTLFSLMQYSDEFRIHFtfndfkrnPSPRSHVSPIKQLN- 222
Cdd:COG1240    89 PQRGRDVVLVVDASGSMAAENrLEAAKGALLDFLDDYRP-RDRVGLVAFGGEAEVLL--------PLTRDREALKRALDe 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  223 ----GRTKTASGIRKVVRELfhktNGARENAAKILVVITDGEKFGDPLDYKDVIPEADRAGVIRYVIGVGNAfnkPQSRR 298
Cdd:COG1240   160 lppgGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE---AVDEG 232

                         170       180       190
                  ....*....|....*....|....*....|
gi 132626289  299 ELDTIASKPAGEHvFQVDNFEALNTIQNQL 328
Cdd:COG1240   233 LLREIAEATGGRY-FRADDLSELAAIYREI 261
VWA_2 pfam13519
von Willebrand factor type A domain;
151-256 2.86e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 61.15  E-value: 2.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289   151 IVFLIDGSGSINNID-----FQKMKEFVSTVMEQFKKSKtlFSLMQYSDEFRIHFTFNdfKRNPSPRSHVSPIKQLNGRT 225
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSLPGDR--VGLVTFGDGPEVLIPLT--KDRAKILRALRRLEPKGGGT 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 132626289   226 KTASGIRKVVRELFHKTNGARenaaKILVVI 256
Cdd:pfam13519   77 NLAAALQLARAALKHRRKNQP----RRIVLI 103
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 517-558 1.13e-10

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: 58.16  E-value: 1.13e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 132626289    517 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEQENQ--GAVYIFYG 558
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFG 44
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 150-297 5.58e-10

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: 60.09  E-value: 5.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  150 DIVFLIDGSGSINNID-FQKMKEFVSTVMEQFKKSK--TLFSLMQYSDEFRIHFTFND-FKRNPSPR----SHVSPIKQL 221
Cdd:cd01471     2 DLYLLVDGSGSIGYSNwVTHVVPFLHTFVQNLNISPdeINLYLVTFSTNAKELIRLSSpNSTNKDLAlnaiRALLSLYYP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 132626289  222 NGRTKTASGIrKVVRELFHKTNGARENAAKILVVITDGEKFGDPLDYKDViPEADRAGVIRYVIGVGNAFNKPQSR 297
Cdd:cd01471    82 NGSTNTTSAL-LVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTLKEA-RKLRERGVIIAVLGVGQGVNHEENR 155
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 521-556 3.59e-08

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 50.20  E-value: 3.59e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 132626289   521 FGAALTVlGDVNGDKLTDVAIGAPGE-QENQGAVYIF 556
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 138-342 3.43e-07

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 53.18  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  138 PEALRECPQQESDIVFLIDGSGSINNIDFQKMKEFVSTVMEQFkKSKTLFSLMQYSDEFRIHFTfndfkrnPSPRSHVSP 217
Cdd:COG2304    81 PPKAAAEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQL-RPGDRVSIVTFAGDARVLLP-------PTPATDRAK 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  218 IK------QLNGRTKTASGIRKVVRELfhkTNGARENAAKILVVITDGE---KFGDPLDYKDVIPEADRAGVIRYVIGVG 288
Cdd:COG2304   153 ILaaidrlQAGGGTALGAGLELAYELA---RKHFIPGRVNRVILLTDGDanvGITDPEELLKLAEEAREEGITLTTLGVG 229

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 132626289  289 NAFNkpqsRRELDTIASKPAGEHVFqVDNFEALntiqnqlqEKIFAIEGTQTGS 342
Cdd:COG2304   230 SDYN----EDLLERLADAGGGNYYY-IDDPEEA--------EKVFVREFSRIGY 270
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 453-495 6.35e-07

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 47.37  E-value: 6.35e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 132626289    453 IGSYFGASLCSV-DMDADGNTNLiLIGAPHYYEKTRGGQVSVCP 495
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDL-LVGAPRANDAGETGAVYVYF 43
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 125-292 1.03e-06

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 51.60  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  125 LFGSNLLRPPQQFPEALRECPQQESDIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKKSKTlFSLMQYSDEFRIHFTFND 204
Cdd:COG2425    95 LALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRR-FGVILFDTEVVEDLPLTA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  205 FKRNPSPRSHVSPIkQLNGRTKTASGIRKVVRELfhktnGARENAAKILVVITDGEkfgDPLDYKDVIPEADRAGV-IR- 282
Cdd:COG2425   174 DDGLEDAIEFLSGL-FAGGGTDIAPALRAALELL-----EEPDYRNADIVLITDGE---AGVSPEELLREVRAKESgVRl 244

                         170
                  ....*....|
gi 132626289  283 YVIGVGNAFN 292
Cdd:COG2425   245 FTVAIGDAGN 254
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 582-620 5.41e-04

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 39.28  E-value: 5.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 132626289    582 QYFGQSLSGGKDLTMDGLMDLAVGA--QGHLLLLRAQPVLR 620
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAprANDAGETGAVYVYF 43
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1131-1143 1.15e-03

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 37.09  E-value: 1.15e-03
                           10
                   ....*....|...
gi 132626289  1131 KLGFFKRQYKDMM 1143
Cdd:pfam00357    1 KCGFFKRNYPPQE 13
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
142-289 5.28e-03

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 39.52  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  142 RECPqqesdIVFLIDGSGSINNIDFQKMKE----FVSTVMEQFKKSKTL-FSLMQYSDEFRIHFTFndfkrnpSPRSHVS 216
Cdd:COG4245     4 RRLP-----VYLLLDTSGSMSGEPIEALNEglqaLIDELRQDPYALETVeVSVITFDGEAKVLLPL-------TDLEDFQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 132626289  217 PIK-QLNGRTKTASGIRKVVREL-----FHKTNGARENaAKILVVITDGEkfgdP--LDYKDVIPEADRA----GVIRYV 284
Cdd:COG4245    72 PPDlSASGGTPLGAALELLLDLIerrvqKYTAEGKGDW-RPVVFLITDGE----PtdSDWEAALQRLKDGeaakKANIFA 146


                  ....*
gi 132626289  285 IGVGN 289
Cdd:COG4245   147 IGVGP 151
 
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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