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Conserved domains on  [gi|442616186|ref|NP_001259505|]
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multiple edematous wings, isoform D [Drosophila melanogaster]

Protein Classification

integrin alpha( domain architecture ID 12192630)

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

CATH:  2.130.10.130|2.60.40.1510|2.60.40.1530|2.60.40.1460
Gene Ontology:  GO:0007155|GO:0008305|GO:0005178|GO:0046872
PubMed:  3028640|2199285|12297042|12826403|14689578|12361595|12234368
SCOP:  4003137

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 392-918 1.77e-131

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: 405.94  E-value: 1.77e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   392 RPIISIQTSVQRKELH-NMDPNTpgClDDPASNLTCFTFRACCSIEPYDEKNKELRLAYSVEAETFDHLKKFSRVFFFDR 470
Cdd:pfam08441    1 RPVVSVSASLQVEPNSiNPEKKN--C-TLTGTPVSCFTVRACFSYTGKPIPNPSLVLNYELELDRQKKKGLPPRVLFLDS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   471 EnkrTNVLSRVVRVHTNGRTECQAVTGYIKANTRDIQTPVRFRLKYSLVEPPLADSALVRLNPILDQTQ-AHVDFEGTFQ 549
Cdd:pfam08441   78 Q---QPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRAPSDLPGLKPILDQNQpSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   550 KDCGDDDLCESNLIIRVEPNITESsgNEYTLILDETELEVRINVSNLADSAYEAQLFIAHQAGVSYVATKKPTN---ATC 626
Cdd:pfam08441  155 KDCGEDNVCVPDLQLSAKFDSRES--DEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSekqLSC 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   627 NSYN---TTLVACSLGNPMLRDTTTFVTIRFQPKGLEPSEKIMLFHIFANTTSKLVGPERPERdLRVNVVRRAKLNFRGW 703
Cdd:pfam08441  233 TAKKensTRQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNSNSNPVS-LKVPVVAEAQLSLSGV 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   704 AIPEQSFYsGSSVANSVANtaatdieghgPMGMDDVGSQVHHMFTIFNEGPSTAPKVQMVIHWPYSLYSDPqsgrpvqYL 783
Cdd:pfam08441  312 SKPDQVVG-GSVKGESAMK----------PRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGK-------WL 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   784 LYLEQVPTveVSQGECHvAKEYVNPLNLasgsrenpaylsapaqmrmfpsqsrhsfNKSLIHSQRSYYSSSHRDDHSDDT 863
Cdd:pfam08441  374 LYLLDVQG--QGKGECS-PQNEINPLNL----------------------------TQSLESSKPLRTSRVHHVVKRRDV 422

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 442616186   864 QSNRNRVRrsflervtrlerlmydpessnaangkkQDIVELDCNKGAtNCVRIEC 918
Cdd:pfam08441  423 LKSEKATQ---------------------------TASVLLSCDSGA-RCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 290-340 3.54e-13

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: 65.09  E-value: 3.54e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 442616186    290 SRFGLALANIGDLNKDNCEDLAVGAPYEGN----GVVYIYLGSSQGLNSKPAQKI 340
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 229-280 1.16e-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: 60.85  E-value: 1.16e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 442616186    229 FGSSFGYELATA-DINGDHRPDLIVAAPLYFTKTEGGAVYVYQNIQDTLPMKY 280
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLLVGAPRANDAGETGAVYVYFGSSGGGNSIP 53
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 358-403 7.20e-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: 38.51  E-value: 7.20e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 442616186    358 FGISISGNTDLDDNSYPDVVIGAFNSSAAVILLARPIISIQTSVQR 403
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGAPRANDAGETGAVYVYFGSSGGGN 50
 
Name Accession Description Interval E-value
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 392-918 1.77e-131

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: 405.94  E-value: 1.77e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   392 RPIISIQTSVQRKELH-NMDPNTpgClDDPASNLTCFTFRACCSIEPYDEKNKELRLAYSVEAETFDHLKKFSRVFFFDR 470
Cdd:pfam08441    1 RPVVSVSASLQVEPNSiNPEKKN--C-TLTGTPVSCFTVRACFSYTGKPIPNPSLVLNYELELDRQKKKGLPPRVLFLDS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   471 EnkrTNVLSRVVRVHTNGRTECQAVTGYIKANTRDIQTPVRFRLKYSLVEPPLADSALVRLNPILDQTQ-AHVDFEGTFQ 549
Cdd:pfam08441   78 Q---QPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRAPSDLPGLKPILDQNQpSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   550 KDCGDDDLCESNLIIRVEPNITESsgNEYTLILDETELEVRINVSNLADSAYEAQLFIAHQAGVSYVATKKPTN---ATC 626
Cdd:pfam08441  155 KDCGEDNVCVPDLQLSAKFDSRES--DEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSekqLSC 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   627 NSYN---TTLVACSLGNPMLRDTTTFVTIRFQPKGLEPSEKIMLFHIFANTTSKLVGPERPERdLRVNVVRRAKLNFRGW 703
Cdd:pfam08441  233 TAKKensTRQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNSNSNPVS-LKVPVVAEAQLSLSGV 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   704 AIPEQSFYsGSSVANSVANtaatdieghgPMGMDDVGSQVHHMFTIFNEGPSTAPKVQMVIHWPYSLYSDPqsgrpvqYL 783
Cdd:pfam08441  312 SKPDQVVG-GSVKGESAMK----------PRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGK-------WL 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   784 LYLEQVPTveVSQGECHvAKEYVNPLNLasgsrenpaylsapaqmrmfpsqsrhsfNKSLIHSQRSYYSSSHRDDHSDDT 863
Cdd:pfam08441  374 LYLLDVQG--QGKGECS-PQNEINPLNL----------------------------TQSLESSKPLRTSRVHHVVKRRDV 422

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 442616186   864 QSNRNRVRrsflervtrlerlmydpessnaangkkQDIVELDCNKGAtNCVRIEC 918
Cdd:pfam08441  423 LKSEKATQ---------------------------TASVLLSCDSGA-RCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 290-340 3.54e-13

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: 65.09  E-value: 3.54e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 442616186    290 SRFGLALANIGDLNKDNCEDLAVGAPYEGN----GVVYIYLGSSQGLNSKPAQKI 340
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 229-280 1.16e-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: 60.85  E-value: 1.16e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 442616186    229 FGSSFGYELATA-DINGDHRPDLIVAAPLYFTKTEGGAVYVYQNIQDTLPMKY 280
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLLVGAPRANDAGETGAVYVYFGSSGGGNSIP 53
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 233-269 1.34e-09

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: 54.05  E-value: 1.34e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 442616186   233 FGYELATADINGDHRPDLIVAAPlYFTKTEGGAVYVY 269
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLAVGAP-GEGGAGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 292-325 1.06e-05

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 43.27  E-value: 1.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 442616186   292 FGLALAnIGDLNKDNCEDLAVGAPYE---GNGVVYIY 325
Cdd:pfam01839    1 FGYSVA-VGDLNGDGYADLAVGAPGEggaGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 358-403 7.20e-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: 38.51  E-value: 7.20e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 442616186    358 FGISISGNTDLDDNSYPDVVIGAFNSSAAVILLARPIISIQTSVQR 403
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGAPRANDAGETGAVYVYFGSSGGGN 50
 
Name Accession Description Interval E-value
Integrin_alpha2 pfam08441
Integrin alpha; This domain is found in integrin alpha and integrin alpha precursors to the C ...
 392-918 1.77e-131

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: 405.94  E-value: 1.77e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   392 RPIISIQTSVQRKELH-NMDPNTpgClDDPASNLTCFTFRACCSIEPYDEKNKELRLAYSVEAETFDHLKKFSRVFFFDR 470
Cdd:pfam08441    1 RPVVSVSASLQVEPNSiNPEKKN--C-TLTGTPVSCFTVRACFSYTGKPIPNPSLVLNYELELDRQKKKGLPPRVLFLDS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   471 EnkrTNVLSRVVRVHTNGRTECQAVTGYIKANTRDIQTPVRFRLKYSLVEPPLADSALVRLNPILDQTQ-AHVDFEGTFQ 549
Cdd:pfam08441   78 Q---QPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDPRAPSDLPGLKPILDQNQpSTVQEQANFL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   550 KDCGDDDLCESNLIIRVEPNITESsgNEYTLILDETELEVRINVSNLADSAYEAQLFIAHQAGVSYVATKKPTN---ATC 626
Cdd:pfam08441  155 KDCGEDNVCVPDLQLSAKFDSRES--DEPLLLGDDNDLALEITVTNLGEDAYEAELYVTLPPGLDYSGVRREGSekqLSC 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   627 NSYN---TTLVACSLGNPMLRDTTTFVTIRFQPKGLEPSEKIMLFHIFANTTSKLVGPERPERdLRVNVVRRAKLNFRGW 703
Cdd:pfam08441  233 TAKKensTRQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRSTNEQNSNSNPVS-LKVPVVAEAQLSLSGV 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   704 AIPEQSFYsGSSVANSVANtaatdieghgPMGMDDVGSQVHHMFTIFNEGPSTAPKVQMVIHWPYSLYSDPqsgrpvqYL 783
Cdd:pfam08441  312 SKPDQVVG-GSVKGESAMK----------PRSEEDIGPLVEHTYEVINNGPSTVSGASLEISWPYELSNGK-------WL 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616186   784 LYLEQVPTveVSQGECHvAKEYVNPLNLasgsrenpaylsapaqmrmfpsqsrhsfNKSLIHSQRSYYSSSHRDDHSDDT 863
Cdd:pfam08441  374 LYLLDVQG--QGKGECS-PQNEINPLNL----------------------------TQSLESSKPLRTSRVHHVVKRRDV 422

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 442616186   864 QSNRNRVRrsflervtrlerlmydpessnaangkkQDIVELDCNKGAtNCVRIEC 918
Cdd:pfam08441  423 LKSEKATQ---------------------------TASVLLSCDSGA-RCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 290-340 3.54e-13

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: 65.09  E-value: 3.54e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 442616186    290 SRFGLALANIGDLNKDNCEDLAVGAPYEGN----GVVYIYLGSSQGLNSKPAQKI 340
Cdd:smart00191    3 SYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 229-280 1.16e-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: 60.85  E-value: 1.16e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 442616186    229 FGSSFGYELATA-DINGDHRPDLIVAAPLYFTKTEGGAVYVYQNIQDTLPMKY 280
Cdd:smart00191    1 PGSYFGYSVAGVgDVNGDGYPDLLVGAPRANDAGETGAVYVYFGSSGGGNSIP 53
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 233-269 1.34e-09

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: 54.05  E-value: 1.34e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 442616186   233 FGYELATADINGDHRPDLIVAAPlYFTKTEGGAVYVY 269
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLAVGAP-GEGGAGAGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 292-325 1.06e-05

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 43.27  E-value: 1.06e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 442616186   292 FGLALAnIGDLNKDNCEDLAVGAPYE---GNGVVYIY 325
Cdd:pfam01839    1 FGYSVA-VGDLNGDGYADLAVGAPGEggaGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 358-403 7.20e-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: 38.51  E-value: 7.20e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 442616186    358 FGISISGNTDLDDNSYPDVVIGAFNSSAAVILLARPIISIQTSVQR 403
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGAPRANDAGETGAVYVYFGSSGGGN 50
 
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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