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Conserved domains on  [gi|1622911363|ref|XP_014981504|]
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integrin alpha-M isoform X3 [Macaca mulatta]

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 ...
 147-322 7.06e-87

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: 278.09  E-value: 7.06e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  147 QDIAFLIDGSGSINPREFQQMKDFVSVMMEQLKK--SKTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSITQLYGRTH 224
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  225 TATAIRKVVRELFNVNQGARKNARKILVVITDGEKFGDPLGyEDVIPEADREGVIRYVIGVGDAFRSSKSRQELNTIASK 304
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                          170
                   ....*....|....*...
gi 1622911363  305 PPRDHVFQVNNFEALKTI 322
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 ...
 614-977 3.99e-38

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: 149.01  E-value: 3.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  614 QPVLRVEATMEFNPREVARNVFECNDQMVKGKeAGEVRVCLRVQKSTRDRlreGQIqsVVTYDLALDSGRPH---SRAVF 690
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS-CFTVRACFSYTGKPIPN---PSL--VLNYELELDRQKKKglpPRVLF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  691 GETKNSTRRQTKTL--GLTQTCETLKLQLPDCIEDPVSPIVLRLNFSLVGTPL--SAFGNLRPVLAEDAQRLFIALFPFE 766
Cdd:pfam08441   75 LDSQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  767 KNCGNDNICQDDLSITFSFMSLDC---LVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLGLSYRKVSRLQNQRSqrswr 843
Cdd:pfam08441  155 KDCGEDNVCVPDLQLSAKFDSRESdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ----- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  844 LACESASSTEVPGALkstsCSINHPiFPENSEVTFNITFDV----DSKASLgnKLLLKANVTSENNMSrTNKTEFQreLP 919
Cdd:pfam08441  230 LSCTAKKENSTRQVV----CDLGNP-MKRGTQVTFGLRFSVsgleLSTEEL--SFDLQIRSTNEQNSN-SNPVSLK--VP 299

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911363  920 VKYAVYMVVT--SHEVSTKY--------INFTASENTSRVMQHQYQVKNLGQRSLP-ISLVFLVPVRLN 977
Cdd:pfam08441  300 VVAEAQLSLSgvSKPDQVVGgsvkgesaMKPRSEEDIGPLVEHTYEVINNGPSTVSgASLEISWPYELS 368
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 515-570 2.33e-11

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 60.08  E-value: 2.33e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622911363   515 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNQ--GAVYLFHGTSGfGISPSHSQRI 570
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSG-GGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 451-508 2.27e-09

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


:

Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 54.30  E-value: 2.27e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911363   451 IGAYFGASLCSV-DVDSNGSTDLVlIGAPYYYEQTRGGQVSVCPLpRAQRGRWQCDAVL 508
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFG-SSGGGNSIPLQNL 57
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1129-1143 3.15e-04

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


:

Pssm-ID: 459778  Cd Length: 15  Bit Score: 38.63  E-value: 3.15e-04
                           10
                   ....*....|....*
gi 1622911363 1129 KLGFFKRQYKDMMSE 1143
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 ...
 147-322 7.06e-87

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: 278.09  E-value: 7.06e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  147 QDIAFLIDGSGSINPREFQQMKDFVSVMMEQLKK--SKTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSITQLYGRTH 224
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  225 TATAIRKVVRELFNVNQGARKNARKILVVITDGEKFGDPLGyEDVIPEADREGVIRYVIGVGDAFRSSKSRQELNTIASK 304
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                          170
                   ....*....|....*...
gi 1622911363  305 PPRDHVFQVNNFEALKTI 322
Cdd:cd01469    160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
148-325 6.27e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 165.91  E-value: 6.27e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQL--KKSKTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSITQLYGRT-H 224
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  225 TATAIRKVVRELFNVNQGARKNARKILVVITDGEK-FGDPlgyEDVIPEADREGVIRYVIGVGDAfrsskSRQELNTIAS 303
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDP---EEVARELKSAGVTVFAVGVGNA-----DDEELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 1622911363  304 KPPRDHVFQVNNFEALKTIQKQ 325
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 148-319 6.93e-42

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: 151.45  E-value: 6.93e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363   148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQLKKS--KTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSIT-QLYGRTH 224
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363   225 TATAIRKVVRELFNVNQGARKNARKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFrsskSRQELNTIASK 304
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV----DEEELKKLASA 156

                           170
                    ....*....|....*
gi 1622911363   305 PPRDHVFQVNNFEAL 319
Cdd:smart00327  157 PGGVYVFLPELLDLL 171
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 614-977 3.99e-38

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: 149.01  E-value: 3.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  614 QPVLRVEATMEFNPREVARNVFECNDQMVKGKeAGEVRVCLRVQKSTRDRlreGQIqsVVTYDLALDSGRPH---SRAVF 690
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS-CFTVRACFSYTGKPIPN---PSL--VLNYELELDRQKKKglpPRVLF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  691 GETKNSTRRQTKTL--GLTQTCETLKLQLPDCIEDPVSPIVLRLNFSLVGTPL--SAFGNLRPVLAEDAQRLFIALFPFE 766
Cdd:pfam08441   75 LDSQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  767 KNCGNDNICQDDLSITFSFMSLDC---LVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLGLSYRKVSRLQNQRSqrswr 843
Cdd:pfam08441  155 KDCGEDNVCVPDLQLSAKFDSRESdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ----- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  844 LACESASSTEVPGALkstsCSINHPiFPENSEVTFNITFDV----DSKASLgnKLLLKANVTSENNMSrTNKTEFQreLP 919
Cdd:pfam08441  230 LSCTAKKENSTRQVV----CDLGNP-MKRGTQVTFGLRFSVsgleLSTEEL--SFDLQIRSTNEQNSN-SNPVSLK--VP 299

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911363  920 VKYAVYMVVT--SHEVSTKY--------INFTASENTSRVMQHQYQVKNLGQRSLP-ISLVFLVPVRLN 977
Cdd:pfam08441  300 VVAEAQLSLSgvSKPDQVVGgsvkgesaMKPRSEEDIGPLVEHTYEVINNGPSTVSgASLEISWPYELS 368
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 515-570 2.33e-11

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 60.08  E-value: 2.33e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622911363   515 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNQ--GAVYLFHGTSGfGISPSHSQRI 570
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSG-GGNSIPLQNL 57
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 142-302 2.03e-09

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 59.57  E-value: 2.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  142 RGCPEQDIAFLIDGSGS--INPReFQQMKDFVSVMMEQLKKsKTLFSLMQYSEE-FW-THFTFeefqrkpNPRSLVNSIT 217
Cdd:COG1240     88 RPQRGRDVVLVVDASGSmaAENR-LEAAKGALLDFLDDYRP-RDRVGLVAFGGEaEVlLPLTR-------DREALKRALD 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  218 QLY--GRTHTATAIRKVVRELfnvnQGARKNARKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAfrsSKSR 295
Cdd:COG1240    159 ELPpgGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE---AVDE 231


                   ....*..
gi 1622911363  296 QELNTIA 302
Cdd:COG1240    232 GLLREIA 238
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 451-508 2.27e-09

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 54.30  E-value: 2.27e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911363   451 IGAYFGASLCSV-DVDSNGSTDLVlIGAPYYYEQTRGGQVSVCPLpRAQRGRWQCDAVL 508
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFG-SSGGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 519-554 5.74e-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: 49.82  E-value: 5.74e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1622911363  519 FGAALTVlGDVNGDKLTDVAIGAPGE-EDNQGAVYLF 554
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 455-491 1.01e-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: 40.57  E-value: 1.01e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1622911363  455 FGASLCSVDVDSNGSTDLVlIGAPYYYEQtRGGQVSV 491
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLA-VGAPGEGGA-GAGAVYV 35
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1129-1143 3.15e-04

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 38.63  E-value: 3.15e-04
                           10
                   ....*....|....*
gi 1622911363 1129 KLGFFKRQYKDMMSE 1143
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 ...
 147-322 7.06e-87

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: 278.09  E-value: 7.06e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  147 QDIAFLIDGSGSINPREFQQMKDFVSVMMEQLKK--SKTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSITQLYGRTH 224
Cdd:cd01469      1 MDIVFVLDGSGSIYPDDFQKVKNFLSTVMKKLDIgpTKTQFGLVQYSESFRTEFTLNEYRTKEEPLSLVKHISQLLGLTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  225 TATAIRKVVRELFNVNQGARKNARKILVVITDGEKFGDPLGyEDVIPEADREGVIRYVIGVGDAFRSSKSRQELNTIASK 304
Cdd:cd01469     81 TATAIQYVVTELFSESNGARKDATKVLVVITDGESHDDPLL-KDVIPQAEREGIIRYAIGVGGHFQRENSREELKTIASK 159

                          170
                   ....*....|....*...
gi 1622911363  305 PPRDHVFQVNNFEALKTI 322
Cdd:cd01469    160 PPEEHFFNVTDFAALKDI 177
VWA pfam00092
von Willebrand factor type A domain;
148-325 6.27e-47

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 165.91  E-value: 6.27e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQL--KKSKTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSITQLYGRT-H 224
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLRYLGGGTtN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  225 TATAIRKVVRELFNVNQGARKNARKILVVITDGEK-FGDPlgyEDVIPEADREGVIRYVIGVGDAfrsskSRQELNTIAS 303
Cdd:pfam00092   81 TGKALKYALENLFSSAAGARPGAPKVVVLLTDGRSqDGDP---EEVARELKSAGVTVFAVGVGNA-----DDEELRKIAS 152

                          170       180
                   ....*....|....*....|..
gi 1622911363  304 KPPRDHVFQVNNFEALKTIQKQ 325
Cdd:pfam00092  153 EPGEGHVFTVSDFEALEDLQDQ 174
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 148-319 6.93e-42

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: 151.45  E-value: 6.93e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363   148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQLKKS--KTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSIT-QLYGRTH 224
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLSyKLGGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363   225 TATAIRKVVRELFNVNQGARKNARKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFrsskSRQELNTIASK 304
Cdd:smart00327   81 LGAALQYALENLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNDV----DEEELKKLASA 156

                           170
                    ....*....|....*
gi 1622911363   305 PPRDHVFQVNNFEAL 319
Cdd:smart00327  157 PGGVYVFLPELLDLL 171
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 614-977 3.99e-38

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: 149.01  E-value: 3.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  614 QPVLRVEATMEFNPREVARNVFECNDQMVKGKeAGEVRVCLRVQKSTRDRlreGQIqsVVTYDLALDSGRPH---SRAVF 690
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTGTPVS-CFTVRACFSYTGKPIPN---PSL--VLNYELELDRQKKKglpPRVLF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  691 GETKNSTRRQTKTL--GLTQTCETLKLQLPDCIEDPVSPIVLRLNFSLVGTPL--SAFGNLRPVLAEDAQRLFIALFPFE 766
Cdd:pfam08441   75 LDSQQPSLTGTLVLlsQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRapSDLPGLKPILDQNQPSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  767 KNCGNDNICQDDLSITFSFMSLDC---LVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLGLSYRKVSRLQNQRSqrswr 843
Cdd:pfam08441  155 KDCGEDNVCVPDLQLSAKFDSRESdepLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSEKQ----- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  844 LACESASSTEVPGALkstsCSINHPiFPENSEVTFNITFDV----DSKASLgnKLLLKANVTSENNMSrTNKTEFQreLP 919
Cdd:pfam08441  230 LSCTAKKENSTRQVV----CDLGNP-MKRGTQVTFGLRFSVsgleLSTEEL--SFDLQIRSTNEQNSN-SNPVSLK--VP 299

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911363  920 VKYAVYMVVT--SHEVSTKY--------INFTASENTSRVMQHQYQVKNLGQRSLP-ISLVFLVPVRLN 977
Cdd:pfam08441  300 VVAEAQLSLSgvSKPDQVVGgsvkgesaMKPRSEEDIGPLVEHTYEVINNGPSTVSgASLEISWPYELS 368
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 148-311 7.46e-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: 133.57  E-value: 7.46e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQLKKS--KTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSITQLYGR-TH 224
Cdd:cd01450      2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGpdKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGgTN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  225 TATAIRKVVRELFNVNQgARKNARKILVVITDGEKFGDPlGYEDVIPEADREGVIRYVIGVGDAfrsskSRQELNTIASK 304
Cdd:cd01450     82 TGKALQYALEQLFSESN-ARENVPKVIIVLTDGRSDDGG-DPKEAAAKLKDEGIKVFVVGVGPA-----DEEELREIASC 154


                   ....*..
gi 1622911363  305 PPRDHVF 311
Cdd:cd01450    155 PSERHVF 161
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 148-316 1.38e-28

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: 112.77  E-value: 1.38e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQLK--KSKTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSITQLYGRTHT 225
Cdd:cd01482      2 DIVFLVDGSWSIGRSNFNLVRSFLSSVVEAFEigPDGVQVGLVQYSDDPRTEFDLNAYTSKEDVLAAIKNLPYKGGNTRT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  226 ATAIRKVVRELFNVNQGARKNARKILVVITDGeKFGDplgyeDVIPEADR---EGVIRYVIGVGDAFRSsksrqELNTIA 302
Cdd:cd01482     82 GKALTHVREKNFTPDAGARPGVPKVVILITDG-KSQD-----DVELPARVlrnLGVNVFAVGVKDADES-----ELKMIA 150

                          170
                   ....*....|....
gi 1622911363  303 SKPPRDHVFQVNNF 316
Cdd:cd01482    151 SKPSETHVFNVADF 164
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 148-316 2.93e-27

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


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 108.85  E-value: 2.93e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQLKKS--KTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSITQLYGRTHT 225
Cdd:cd01472      2 DIVFLVDGSESIGLSNFNLVKDFVKRVVERLDIGpdGVRVGVVQYSDDPRTEFYLNTYRSKDDVLEAVKNLRYIGGGTNT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  226 ATAIRKVVRELFNVNQGARKNARKILVVITDGEKfgdplgYEDVIPEAD---REGVIRYVIGVGDAfrsskSRQELNTIA 302
Cdd:cd01472     82 GKALKYVRENLFTEASGSREGVPKVLVVITDGKS------QDDVEEPAVelkQAGIEVFAVGVKNA-----DEEELKQIA 150

                          170
                   ....*....|....
gi 1622911363  303 SKPPRDHVFQVNNF 316
Cdd:cd01472    151 SDPKELYVFNVADF 164
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 148-330 5.35e-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: 5.35e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQLKKSK--TLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSITQLYGRTHT 225
Cdd:cd01475      4 DLVFLIDSSRSVRPENFELVKQFLNQIIDSLDVGPdaTRVGLVQYSSTVKQEFPLGRFKSKADLKRAVRRMEYLETGTMT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  226 ATAIRKVVRELFNVNQGARK---NARKILVVITDGEKfGDPLGyeDVIPEADREGVIRYVIGVGDAFRSsksrqELNTIA 302
Cdd:cd01475     84 GLAIQYAMNNAFSEAEGARPgseRVPRVGIVVTDGRP-QDDVS--EVAAKARALGIEMFAVGVGRADEE-----ELREIA 155

                          170       180
                   ....*....|....*....|....*...
gi 1622911363  303 SKPPRDHVFQVNNFEALKTIQKQLQEKI 330
Cdd:cd01475    156 SEPLADHVFYVEDFSTIEELTKKFQGKI 183
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 148-311 1.58e-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: 106.88  E-value: 1.58e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQLKKS--KTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSIT-QLYGRTH 224
Cdd:cd00198      2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASppGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKkGLGGGTN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  225 TATAIRKVVRELfnvNQGARKNARKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDafrsSKSRQELNTIASK 304
Cdd:cd00198     82 IGAALRLALELL---KSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIGD----DANEDELKEIADK 154


                   ....*..
gi 1622911363  305 PPRDHVF 311
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 ...
 148-316 1.05e-14

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


Pssm-ID: 238758  Cd Length: 165  Bit Score: 73.13  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQLK--KSKTLFSLMQYSEEFWTHFTFEEFQRKpnpRSLVNSITQLYGRT-- 223
Cdd:cd01481      2 DIVFLIDGSDNVGSGNFPAIRDFIERIVQSLDvgPDKIRVAVVQFSDTPRPEFYLNTHSTK---ADVLGAVRRLRLRGgs 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  224 --HTATAIRKVVRELFNVNQGAR--KNARKILVVITDGEKFGDplgYEDVIPEADREGVIRYVIGVGDAfrsskSRQELN 299
Cdd:cd01481     79 qlNTGSALDYVVKNLFTKSAGSRieEGVPQFLVLITGGKSQDD---VERPAVALKRAGIVPFAIGARNA-----DLAELQ 150

                          170
                   ....*....|....*..
gi 1622911363  300 TIASKPprDHVFQVNNF 316
Cdd:cd01481    151 QIAFDP--SFVFQVSDF 165
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 148-311 1.52e-14

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


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 72.43  E-value: 1.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINPReFQQMKDFVSVMMEQLK--KSKTLFSLMQYSEEFWTH--FTFEEFQRKPNPRSLVNSITQLYGRT 223
Cdd:cd01476      2 DLLFVLDSSGSVRGK-FEKYKKYIERIVEGLEigPTATRVALITYSGRGRQRvrFNLPKHNDGEELLEKVDNLRFIGGTT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  224 HTATAIRKVVrELFNVNQGARKNARKILVVITDGEKFGDPLGyedvIPEADREGVIRYVIGVGDAFRSSKSRQELNTIAS 303
Cdd:cd01476     81 ATGAAIEVAL-QQLDPSEGRREGIPKVVVVLTDGRSHDDPEK----QARILRAVPNIETFAVGTGDPGTVDTEELHSITG 155


                   ....*...
gi 1622911363  304 KPprDHVF 311
Cdd:cd01476    156 NE--DHIF 161
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 148-322 4.11e-14

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: 71.77  E-value: 4.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINpREFQQMKDFVSVMMEQLKKSKTLFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSITQLYGRTHTAT 227
Cdd:cd01474      6 DLYFVLDKSGSVA-ANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQTYIHE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  228 AIRKVVRELFNVNQGARKNArKILVVITDGEKFGDPLGY-EDVIPEADREGVIRYVIGVGDAfrsskSRQELNTIASKPp 306
Cdd:cd01474     85 GLENANEQIFNRNGGGRETV-SVIIALTDGQLLLNGHKYpEHEAKLSRKLGAIVYCVGVTDF-----LKSQLINIADSK- 157

                          170
                   ....*....|....*..
gi 1622911363  307 rDHVFQVNN-FEALKTI 322
Cdd:cd01474    158 -EYVFPVTSgFQALSGI 173
VWA_2 pfam13519
von Willebrand factor type A domain;
149-254 1.42e-11

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 61.92  E-value: 1.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  149 IAFLIDGSGSIN-----PREFQQMKDFVSVMMEQLKKSKtlFSLMQYSEEFWTHFTFEEFQRKPnpRSLVNSITQLYGRT 223
Cdd:pfam13519    1 LVFVLDTSGSMRngdygPTRLEAAKDAVLALLKSLPGDR--VGLVTFGDGPEVLIPLTKDRAKI--LRALRRLEPKGGGT 76

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1622911363  224 HTATAIRKVVRELfnvnQGARKNARKILVVI 254
Cdd:pfam13519   77 NLAAALQLARAAL----KHRRKNQPRRIVLI 103
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 515-570 2.33e-11

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 60.08  E-value: 2.33e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622911363   515 PWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNQ--GAVYLFHGTSGfGISPSHSQRI 570
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAGetGAVYVYFGSSG-GGNSIPLQNL 57
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 144-319 6.68e-11

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


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 62.40  E-value: 6.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  144 CPeQDIAFLIDGSGSINPREFQQMKDFVSVMMEQLKKSKTL--------FSLMQYSEEfwthfTFEEFQRKPNPRSL--- 212
Cdd:cd01480      1 GP-VDITFVLDSSESVGLQNFDITKNFVKRVAERFLKDYYRkdpagswrVGVVQYSDQ-----QEVEAGFLRDIRNYtsl 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  213 ---VNSITQLYGRTHTATAIRKVVRELFnvnQGARKNARKILVVITDGEKFG-DPLGYEDVIPEADREGVIRYVIGVGda 288
Cdd:cd01480     75 keaVDNLEYIGGGTFTDCALKYATEQLL---EGSHQKENKFLLVITDGHSDGsPDGGIEKAVNEADHLGIKIFFVAVG-- 149

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1622911363  289 frsSKSRQELNTIASKPPRDHvfQVNNFEAL 319
Cdd:cd01480    150 ---SQNEEPLSRIACDGKSAL--YRENFAEL 175
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 142-302 2.03e-09

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 59.57  E-value: 2.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  142 RGCPEQDIAFLIDGSGS--INPReFQQMKDFVSVMMEQLKKsKTLFSLMQYSEE-FW-THFTFeefqrkpNPRSLVNSIT 217
Cdd:COG1240     88 RPQRGRDVVLVVDASGSmaAENR-LEAAKGALLDFLDDYRP-RDRVGLVAFGGEaEVlLPLTR-------DREALKRALD 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  218 QLY--GRTHTATAIRKVVRELfnvnQGARKNARKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAfrsSKSR 295
Cdd:COG1240    159 ELPpgGGTPLGDALALALELL----KRADPARRKVIVLLTDGRDNAGRIDPLEAAELAAAAGIRIYTIGVGTE---AVDE 231


                   ....*..
gi 1622911363  296 QELNTIA 302
Cdd:COG1240    232 GLLREIA 238
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 451-508 2.27e-09

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


Pssm-ID: 214549 [Multi-domain]  Cd Length: 57  Bit Score: 54.30  E-value: 2.27e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911363   451 IGAYFGASLCSV-DVDSNGSTDLVlIGAPYYYEQTRGGQVSVCPLpRAQRGRWQCDAVL 508
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLL-VGAPRANDAGETGAVYVYFG-SSGGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 519-554 5.74e-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: 49.82  E-value: 5.74e-08
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1622911363  519 FGAALTVlGDVNGDKLTDVAIGAPGE-EDNQGAVYLF 554
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGEgGAGAGAVYVL 36
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 148-295 1.30e-07

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


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 53.16  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSIN-PREFQQMKDFVSVMMEQLKKSK-------TLFSlmQYSEEFWTHFTFeefqRKPNPRSLVNSITQL 219
Cdd:cd01471      2 DLYLLVDGSGSIGySNWVTHVVPFLHTFVQNLNISPdeinlylVTFS--TNAKELIRLSSP----NSTNKDLALNAIRAL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  220 ------YGRTHTATAIrKVVRELFNVNQGARKNARKILVVITDGEKFGDPLGYEDVIPEADReGVIRYVIGVGDAFRSSK 293
Cdd:cd01471     76 lslyypNGSTNTTSAL-LVVEKHLFDTRGNRENAPQLVIIMTDGIPDSKFRTLKEARKLRER-GVIIAVLGVGQGVNHEE 153


                   ..
gi 1622911363  294 SR 295
Cdd:cd01471    154 NR 155
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 148-304 2.58e-06

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 50.49  E-value: 2.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  148 DIAFLIDGSGSINPREFQQMKDFVSVMMEQLkKSKTLFSLMQYSEEFWTHFtfeEFQRKPNPRSLVNSITQLY--GRTHT 225
Cdd:COG2304     93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQL-RPGDRVSIVTFAGDARVLL---PPTPATDRAKILAAIDRLQagGGTAL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  226 ATAIRKVVRELfnvNQGARKNARKILVVITDGE---KFGDPLGYEDVIPEADREGVIRYVIGVGDAFRssksRQELNTIA 302
Cdd:COG2304    169 GAGLELAYELA---RKHFIPGRVNRVILLTDGDanvGITDPEELLKLAEEAREEGITLTTLGVGSDYN----EDLLERLA 241


                   ..
gi 1622911363  303 SK 304
Cdd:COG2304    242 DA 243
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 145-288 6.34e-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: 49.29  E-value: 6.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  145 PEQDIAFLIDGSGSINPREFQQMKDFVSVMMEQLKKSKTlFSLMQYSEEFWTHFTFEEFQRKPNPRSLVNSItQLYGRTH 224
Cdd:COG2425    117 LEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRR-FGVILFDTEVVEDLPLTADDGLEDAIEFLSGL-FAGGGTD 194

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622911363  225 TATAIRKVVRELfnvnqGARKNARKILVVITDGEkfgDPLGYEDVIPEAD-REGVIR-YVIGVGDA 288
Cdd:COG2425    195 IAPALRAALELL-----EEPDYRNADIVLITDGE---AGVSPEELLREVRaKESGVRlFTVAIGDA 252
vWA_norD_type cd01454
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ...
 149-294 4.82e-05

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: 45.01  E-value: 4.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  149 IAFLIDGSGS-INPREFQQMKDFVSVMMEQLKKSKTLFSLMQYSE-------EFWTHF-TFEE-FQRKPNPRslvnsITQ 218
Cdd:cd01454      3 VTLLLDLSGSmRSDRRIDVAKKAAVLLAEALEACGVPHAILGFTTdaggrerVRWIKIkDFDEsLHERARKR-----LAA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  219 LYGR--THTATAIRKVVRELfnvnqGARKNARKILVVITDGEKF------GDPLGYED---VIPEADREGVIRYVIGVG- 286
Cdd:cd01454     78 LSPGgnTRDGAAIRHAAERL-----LARPEKRKILLVISDGEPNdldyyeGNVFATEDalrAVIEARKLGIEVFGITIDr 152


                   ....*...
gi 1622911363  287 DAFRSSKS 294
Cdd:cd01454    153 DATTVDKE 160
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 455-491 1.01e-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: 40.57  E-value: 1.01e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1622911363  455 FGASLCSVDVDSNGSTDLVlIGAPYYYEQtRGGQVSV 491
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLA-VGAPGEGGA-GAGAVYV 35
Integrin_alpha pfam00357
Integrin alpha cytoplasmic region; This family contains the short intracellular region of ...
 1129-1143 3.15e-04

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


Pssm-ID: 459778  Cd Length: 15  Bit Score: 38.63  E-value: 3.15e-04
                           10
                   ....*....|....*
gi 1622911363 1129 KLGFFKRQYKDMMSE 1143
Cdd:pfam00357    1 KCGFFKRNYPPQEEE 15
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
142-287 5.81e-04

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 42.22  E-value: 5.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  142 RGCPeqdIAFLIDGSGSINPREFQQMKDFVSVMMEQLKKSKTL-----FSLMQYSEEFWTHFTF---EEFQrkpnPRSLV 213
Cdd:COG4245      4 RRLP---VYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPYAletveVSVITFDGEAKVLLPLtdlEDFQ----PPDLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911363  214 NSitqlyGRTHTATAIRKVVRELFNVNQGARKNA----RKILVVITDGEkfgdP--LGYEDVIPEADR----EGVIRYVI 283
Cdd:COG4245     77 AS-----GGTPLGAALELLLDLIERRVQKYTAEGkgdwRPVVFLITDGE----PtdSDWEAALQRLKDgeaaKKANIFAI 147


                   ....
gi 1622911363  284 GVGD 287
Cdd:COG4245    148 GVGP 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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