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Conserved domains on  [gi|1039732199|ref|XP_017169302|]
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integrin alpha-7 isoform X1 [Mus musculus]

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 ...
 476-965 6.11e-157

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: 474.12  E-value: 6.11e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  476 RPVLHVSQEIFIDPRAIDLEQPNCADG--RLVCVDIKICFSYVAVPSsYSPSVALDYMLDGDTDRRlRGQVPRVTFLsrg 553
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTgtPVSCFTVRACFSYTGKPI-PNPSLVLNYELELDRQKK-KGLPPRVLFL--- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  554 lDDLRHQSSGTVWLKHQHDRVCGDTVFQLQENVKDKLRAIVVTLSYGLRTPPlgrqAPGQELPTVAPILNAHQPSTQRTE 633
Cdd:pfam08441   76 -DSQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDP----RAPSDLPGLKPILDQNQPSTVQEQ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  634 IHFLKQgCGEDKICQSNLQLErYQFCSRISDTEFqalpmdldgrtalfALSGQPFIGLELTVTNlpsdparpqaDGDDAH 713
Cdd:pfam08441  151 ANFLKD-CGEDNVCVPDLQLS-AKFDSRESDEPL--------------LLGDDNDLALEITVTN----------LGEDAY 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  714 EAQLLVTLPASLRYSGVRALDSVEKPLCLSNDSAS--HVECELGNPMKRGAQVTFYLILSTSGITIETTELEVKLLLATI 791
Cdd:pfam08441  205 EAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRST 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  792 SEQE--LDPVSVRAHVFIELPLSISGVATPQQLFFsGEVKGESAM--RSERDVGSKVKYEVTVSNQGQSlnTLGSAFLNI 867
Cdd:pfam08441  285 NEQNsnSNPVSLKVPVVAEAQLSLSGVSKPDQVVG-GSVKGESAMkpRSEEDIGPLVEHTYEVINNGPS--TVSGASLEI 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  868 MWPHEIANGKWLLYPMRVElegGQGPGKrgiCSPRPNILQLDVDSRDRRRRELGQPEPQEPPEKVEPSTSWWPVSSAekr 947
Cdd:pfam08441  362 SWPYELSNGKWLLYLLDVQ---GQGKGE---CSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTA--- 432

                          490
                   ....*....|....*...
gi 1039732199  948 NVTLDCAQGtAKCVVFSC 965
Cdd:pfam08441  433 SVLLSCDSG-ARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 381-433 3.43e-15

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: 70.87  E-value: 3.43e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039732199   381 PDSMFGISLAVLGDLNQDGFPDIAVGAPFDGD----GKVFIYHGSSLGVVVKPSQVL 433
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 322-375 1.08e-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: 1.08e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039732199   322 SGFGYSLA-VTDLNNDGWADLIVGAPYFFERQEelGGAVYVYMNQ--GGHWADISPL 375
Cdd:smart00191    3 SYFGYSVAgVGDVNGDGYPDLLVGAPRANDAGE--TGAVYVYFGSsgGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 48-109 3.49e-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: 48.14  E-value: 3.49e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039732199    48 PGSLFGFSVALHRQLQPRPQSWLLVGAPQAlalpgQQANRTGGLFACPLSLEETDCYRVDID 109
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRA-----NDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 443-483 1.88e-05

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: 43.13  E-value: 1.88e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1039732199   443 FGYSLSGGLDVDGNHYPDLLVGS-LADTAALFRARPVLHVSQ 483
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGApRANDAGETGAVYVYFGSS 46
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 263-315 1.78e-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: 40.44  E-value: 1.78e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039732199   263 ANSYLGFSIDSGKGLMRSEELSFVAGAPRANHK---GAVVILRKDS-ASRLIPEVVL 315
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAgetGAVYVYFGSSgGGNSIPLQNL 57
 
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 ...
 476-965 6.11e-157

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: 474.12  E-value: 6.11e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  476 RPVLHVSQEIFIDPRAIDLEQPNCADG--RLVCVDIKICFSYVAVPSsYSPSVALDYMLDGDTDRRlRGQVPRVTFLsrg 553
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTgtPVSCFTVRACFSYTGKPI-PNPSLVLNYELELDRQKK-KGLPPRVLFL--- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  554 lDDLRHQSSGTVWLKHQHDRVCGDTVFQLQENVKDKLRAIVVTLSYGLRTPPlgrqAPGQELPTVAPILNAHQPSTQRTE 633
Cdd:pfam08441   76 -DSQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDP----RAPSDLPGLKPILDQNQPSTVQEQ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  634 IHFLKQgCGEDKICQSNLQLErYQFCSRISDTEFqalpmdldgrtalfALSGQPFIGLELTVTNlpsdparpqaDGDDAH 713
Cdd:pfam08441  151 ANFLKD-CGEDNVCVPDLQLS-AKFDSRESDEPL--------------LLGDDNDLALEITVTN----------LGEDAY 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  714 EAQLLVTLPASLRYSGVRALDSVEKPLCLSNDSAS--HVECELGNPMKRGAQVTFYLILSTSGITIETTELEVKLLLATI 791
Cdd:pfam08441  205 EAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRST 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  792 SEQE--LDPVSVRAHVFIELPLSISGVATPQQLFFsGEVKGESAM--RSERDVGSKVKYEVTVSNQGQSlnTLGSAFLNI 867
Cdd:pfam08441  285 NEQNsnSNPVSLKVPVVAEAQLSLSGVSKPDQVVG-GSVKGESAMkpRSEEDIGPLVEHTYEVINNGPS--TVSGASLEI 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  868 MWPHEIANGKWLLYPMRVElegGQGPGKrgiCSPRPNILQLDVDSRDRRRRELGQPEPQEPPEKVEPSTSWWPVSSAekr 947
Cdd:pfam08441  362 SWPYELSNGKWLLYLLDVQ---GQGKGE---CSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTA--- 432

                          490
                   ....*....|....*...
gi 1039732199  948 NVTLDCAQGtAKCVVFSC 965
Cdd:pfam08441  433 SVLLSCDSG-ARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 381-433 3.43e-15

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: 70.87  E-value: 3.43e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039732199   381 PDSMFGISLAVLGDLNQDGFPDIAVGAPFDGD----GKVFIYHGSSLGVVVKPSQVL 433
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 322-375 1.08e-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: 1.08e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039732199   322 SGFGYSLA-VTDLNNDGWADLIVGAPYFFERQEelGGAVYVYMNQ--GGHWADISPL 375
Cdd:smart00191    3 SYFGYSVAgVGDVNGDGYPDLLVGAPRANDAGE--TGAVYVYFGSsgGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 324-362 1.85e-10

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: 56.75  E-value: 1.85e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1039732199  324 FGYSLAVTDLNNDGWADLIVGAPYFFERQeelGGAVYVY 362
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLAVGAPGEGGAG---AGAVYVL 36
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 385-418 1.14e-07

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 48.66  E-value: 1.14e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1039732199  385 FGISLAVlGDLNQDGFPDIAVGAPF---DGDGKVFIY 418
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGeggAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 48-109 3.49e-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: 48.14  E-value: 3.49e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039732199    48 PGSLFGFSVALHRQLQPRPQSWLLVGAPQAlalpgQQANRTGGLFACPLSLEETDCYRVDID 109
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRA-----NDAGETGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 443-483 1.88e-05

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: 43.13  E-value: 1.88e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1039732199   443 FGYSLSGGLDVDGNHYPDLLVGS-LADTAALFRARPVLHVSQ 483
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGApRANDAGETGAVYVYFGSS 46
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 263-315 1.78e-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: 40.44  E-value: 1.78e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039732199   263 ANSYLGFSIDSGKGLMRSEELSFVAGAPRANHK---GAVVILRKDS-ASRLIPEVVL 315
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAgetGAVYVYFGSSgGGNSIPLQNL 57
 
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 ...
 476-965 6.11e-157

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: 474.12  E-value: 6.11e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  476 RPVLHVSQEIFIDPRAIDLEQPNCADG--RLVCVDIKICFSYVAVPSsYSPSVALDYMLDGDTDRRlRGQVPRVTFLsrg 553
Cdd:pfam08441    1 RPVVSVSASLQVEPNSINPEKKNCTLTgtPVSCFTVRACFSYTGKPI-PNPSLVLNYELELDRQKK-KGLPPRVLFL--- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  554 lDDLRHQSSGTVWLKHQHDRVCGDTVFQLQENVKDKLRAIVVTLSYGLRTPPlgrqAPGQELPTVAPILNAHQPSTQRTE 633
Cdd:pfam08441   76 -DSQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDP----RAPSDLPGLKPILDQNQPSTVQEQ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  634 IHFLKQgCGEDKICQSNLQLErYQFCSRISDTEFqalpmdldgrtalfALSGQPFIGLELTVTNlpsdparpqaDGDDAH 713
Cdd:pfam08441  151 ANFLKD-CGEDNVCVPDLQLS-AKFDSRESDEPL--------------LLGDDNDLALEITVTN----------LGEDAY 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  714 EAQLLVTLPASLRYSGVRALDSVEKPLCLSNDSAS--HVECELGNPMKRGAQVTFYLILSTSGITIETTELEVKLLLATI 791
Cdd:pfam08441  205 EAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRST 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  792 SEQE--LDPVSVRAHVFIELPLSISGVATPQQLFFsGEVKGESAM--RSERDVGSKVKYEVTVSNQGQSlnTLGSAFLNI 867
Cdd:pfam08441  285 NEQNsnSNPVSLKVPVVAEAQLSLSGVSKPDQVVG-GSVKGESAMkpRSEEDIGPLVEHTYEVINNGPS--TVSGASLEI 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  868 MWPHEIANGKWLLYPMRVElegGQGPGKrgiCSPRPNILQLDVDSRDRRRRELGQPEPQEPPEKVEPSTSWWPVSSAekr 947
Cdd:pfam08441  362 SWPYELSNGKWLLYLLDVQ---GQGKGE---CSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTA--- 432

                          490
                   ....*....|....*...
gi 1039732199  948 NVTLDCAQGtAKCVVFSC 965
Cdd:pfam08441  433 SVLLSCDSG-ARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 381-433 3.43e-15

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: 70.87  E-value: 3.43e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039732199   381 PDSMFGISLAVLGDLNQDGFPDIAVGAPFDGD----GKVFIYHGSSLGVVVKPSQVL 433
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 322-375 1.08e-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: 1.08e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039732199   322 SGFGYSLA-VTDLNNDGWADLIVGAPYFFERQEelGGAVYVYMNQ--GGHWADISPL 375
Cdd:smart00191    3 SYFGYSVAgVGDVNGDGYPDLLVGAPRANDAGE--TGAVYVYFGSsgGGNSIPLQNL 57
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 324-362 1.85e-10

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: 56.75  E-value: 1.85e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1039732199  324 FGYSLAVTDLNNDGWADLIVGAPYFFERQeelGGAVYVY 362
Cdd:pfam01839    1 FGYSVAVGDLNGDGYADLAVGAPGEGGAG---AGAVYVL 36
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 332-405 1.48e-09

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 54.92  E-value: 1.48e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039732199  332 DLNNDGWADLIVGAPyfferqeelgGAVYVYMNQG-GHWADISPLRIcgsPDSMFGISLAVlGDLNQDGFPDIAV 405
Cdd:pfam13517    1 DLDGDGKLDLVVAND----------GGLRLYLNNGdGTFTFITSVSL---GGGGGGLSVAV-GDLDGDGRLDLLV 61
FG-GAP pfam01839
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
 385-418 1.14e-07

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


Pssm-ID: 460357  Cd Length: 36  Bit Score: 48.66  E-value: 1.14e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1039732199  385 FGISLAVlGDLNQDGFPDIAVGAPF---DGDGKVFIY 418
Cdd:pfam01839    1 FGYSVAV-GDLNGDGYADLAVGAPGeggAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 48-109 3.49e-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: 48.14  E-value: 3.49e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039732199    48 PGSLFGFSVALHRQLQPRPQSWLLVGAPQAlalpgQQANRTGGLFACPLSLEETDCYRVDID 109
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRA-----NDAGETGAVYVYFGSSGGGNSIPLQNL 57
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 394-463 5.50e-06

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 44.91  E-value: 5.50e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039732199  394 DLNQDGFPDIAVGapfdGDGKVFIYHGSSLGVVVKPSQVlegeAVGIKSFGYSLSGGlDVDGNHYPDLLV 463
Cdd:pfam13517    1 DLDGDGKLDLVVA----NDGGLRLYLNNGDGTFTFITSV----SLGGGGGGLSVAVG-DLDGDGRLDLLV 61
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 443-483 1.88e-05

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: 43.13  E-value: 1.88e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1039732199   443 FGYSLSGGLDVDGNHYPDLLVGS-LADTAALFRARPVLHVSQ 483
Cdd:smart00191    5 FGYSVAGVGDVNGDGYPDLLVGApRANDAGETGAVYVYFGSS 46
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 263-315 1.78e-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: 40.44  E-value: 1.78e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039732199   263 ANSYLGFSIDSGKGLMRSEELSFVAGAPRANHK---GAVVILRKDS-ASRLIPEVVL 315
Cdd:smart00191    1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAgetGAVYVYFGSSgGGNSIPLQNL 57
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 293-343 9.98e-03

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.


Pssm-ID: 433275 [Multi-domain]  Cd Length: 61  Bit Score: 35.66  E-value: 9.98e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039732199  293 NHKGAVVILRKDSASRLIPEVVLSgerlTSGFGYSLAVTDLNNDGWADLIV 343
Cdd:pfam13517   15 DGGLRLYLNNGDGTFTFITSVSLG----GGGGGLSVAVGDLDGDGRLDLLV 61
 
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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