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Conserved domains on  [gi|1720360523|ref|XP_030100774|]
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integrin alpha-7 isoform X4 [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 ...
 309-798 2.08e-158

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: 473.73  E-value: 2.08e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 309 RPVLHVSQEIFIDPRAIDLEQPNCADG--RLVCVDIKICFSYVAVPSsYSPSVALDYMLDGDTDRRlRGQVPRVTFLsrg 386
Cdd:pfam08441   1 RPVVSVSASLQVEPNSINPEKKNCTLTgtPVSCFTVRACFSYTGKPI-PNPSLVLNYELELDRQKK-KGLPPRVLFL--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 387 lDDLRHQSSGTVWLKHQHDRVCGDTVFQLQENVKDKLRAIVVTLSYGLRTPPlgrqAPGQELPTVAPILNAHQPSTQRTE 466
Cdd:pfam08441  76 -DSQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDP----RAPSDLPGLKPILDQNQPSTVQEQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 467 IHFLKQgCGEDKICQSNLQLErYQFCSRISDTEFqalpmdldgrtalfALSGQPFIGLELTVTNlpsdparpqaDGDDAH 546
Cdd:pfam08441 151 ANFLKD-CGEDNVCVPDLQLS-AKFDSRESDEPL--------------LLGDDNDLALEITVTN----------LGEDAY 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 547 EAQLLVTLPASLRYSGVRALDSVEKPLCLSNDSAS--HVECELGNPMKRGAQVTFYLILSTSGITIETTELEVKLLLATI 624
Cdd:pfam08441 205 EAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRST 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 625 SEQE--LDPVSVRAHVFIELPLSISGVATPQQLFFsGEVKGESAM--RSERDVGSKVKYEVTVSNQGQSlnTLGSAFLNI 700
Cdd:pfam08441 285 NEQNsnSNPVSLKVPVVAEAQLSLSGVSKPDQVVG-GSVKGESAMkpRSEEDIGPLVEHTYEVINNGPS--TVSGASLEI 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 701 MWPHEIANGKWLLYPMRVElegGQGPGKrgiCSPRPNILQLDVDSRDRRRRELGQPEPQEPPEKVEPSTSWWPVSSAekr 780
Cdd:pfam08441 362 SWPYELSNGKWLLYLLDVQ---GQGKGE---CSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTA--- 432

                         490
                  ....*....|....*...
gi 1720360523 781 NVTLDCAQGtAKCVVFSC 798
Cdd:pfam08441 433 SVLLSCDSG-ARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 214-266 1.82e-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: 71.25  E-value: 1.82e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360523  214 PDSMFGISLAVLGDLNQDGFPDIAVGAPFDGD----GKVFIYHGSSLGVVVKPSQVL 266
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 155-208 6.48e-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: 58.54  E-value: 6.48e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360523  155 SGFGYSLA-VTDLNNDGWADLIVGAPYFFERQEelGGAVYVYMNQ--GGHWADISPL 208
Cdd:smart00191   3 SYFGYSVAgVGDVNGDGYPDLLVGAPRANDAGE--TGAVYVYFGSsgGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 276-316 1.23e-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: 43.52  E-value: 1.23e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1720360523  276 FGYSLSGGLDVDGNHYPDLLVGS-LADTAALFRARPVLHVSQ 316
Cdd:smart00191   5 FGYSVAGVGDVNGDGYPDLLVGApRANDAGETGAVYVYFGSS 46
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 97-148 1.53e-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: 1.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360523   97 NSYLGFSIDSGKGLMRSEELSFVAGAPRANHK---GAVVILRKDS-ASRLIPEVVL 148
Cdd:smart00191   2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAgetGAVYVYFGSSgGGNSIPLQNL 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 ...
 309-798 2.08e-158

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: 473.73  E-value: 2.08e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 309 RPVLHVSQEIFIDPRAIDLEQPNCADG--RLVCVDIKICFSYVAVPSsYSPSVALDYMLDGDTDRRlRGQVPRVTFLsrg 386
Cdd:pfam08441   1 RPVVSVSASLQVEPNSINPEKKNCTLTgtPVSCFTVRACFSYTGKPI-PNPSLVLNYELELDRQKK-KGLPPRVLFL--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 387 lDDLRHQSSGTVWLKHQHDRVCGDTVFQLQENVKDKLRAIVVTLSYGLRTPPlgrqAPGQELPTVAPILNAHQPSTQRTE 466
Cdd:pfam08441  76 -DSQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDP----RAPSDLPGLKPILDQNQPSTVQEQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 467 IHFLKQgCGEDKICQSNLQLErYQFCSRISDTEFqalpmdldgrtalfALSGQPFIGLELTVTNlpsdparpqaDGDDAH 546
Cdd:pfam08441 151 ANFLKD-CGEDNVCVPDLQLS-AKFDSRESDEPL--------------LLGDDNDLALEITVTN----------LGEDAY 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 547 EAQLLVTLPASLRYSGVRALDSVEKPLCLSNDSAS--HVECELGNPMKRGAQVTFYLILSTSGITIETTELEVKLLLATI 624
Cdd:pfam08441 205 EAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRST 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 625 SEQE--LDPVSVRAHVFIELPLSISGVATPQQLFFsGEVKGESAM--RSERDVGSKVKYEVTVSNQGQSlnTLGSAFLNI 700
Cdd:pfam08441 285 NEQNsnSNPVSLKVPVVAEAQLSLSGVSKPDQVVG-GSVKGESAMkpRSEEDIGPLVEHTYEVINNGPS--TVSGASLEI 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 701 MWPHEIANGKWLLYPMRVElegGQGPGKrgiCSPRPNILQLDVDSRDRRRRELGQPEPQEPPEKVEPSTSWWPVSSAekr 780
Cdd:pfam08441 362 SWPYELSNGKWLLYLLDVQ---GQGKGE---CSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTA--- 432

                         490
                  ....*....|....*...
gi 1720360523 781 NVTLDCAQGtAKCVVFSC 798
Cdd:pfam08441 433 SVLLSCDSG-ARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 214-266 1.82e-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: 71.25  E-value: 1.82e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360523  214 PDSMFGISLAVLGDLNQDGFPDIAVGAPFDGD----GKVFIYHGSSLGVVVKPSQVL 266
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 155-208 6.48e-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: 58.54  E-value: 6.48e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360523  155 SGFGYSLA-VTDLNNDGWADLIVGAPYFFERQEelGGAVYVYMNQ--GGHWADISPL 208
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 ...
 157-195 1.65e-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: 1.65e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720360523 157 FGYSLAVTDLNNDGWADLIVGAPYFFERQeelGGAVYVY 195
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 ...
 218-251 1.02e-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: 1.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720360523 218 FGISLAVlGDLNQDGFPDIAVGAPF---DGDGKVFIY 251
Cdd:pfam01839   1 FGYSVAV-GDLNGDGYADLAVGAPGeggAGAGAVYVL 36
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 276-316 1.23e-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: 43.52  E-value: 1.23e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1720360523  276 FGYSLSGGLDVDGNHYPDLLVGS-LADTAALFRARPVLHVSQ 316
Cdd:smart00191   5 FGYSVAGVGDVNGDGYPDLLVGApRANDAGETGAVYVYFGSS 46
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 97-148 1.53e-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: 1.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360523   97 NSYLGFSIDSGKGLMRSEELSFVAGAPRANHK---GAVVILRKDS-ASRLIPEVVL 148
Cdd:smart00191   2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAgetGAVYVYFGSSgGGNSIPLQNL 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 ...
 309-798 2.08e-158

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: 473.73  E-value: 2.08e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 309 RPVLHVSQEIFIDPRAIDLEQPNCADG--RLVCVDIKICFSYVAVPSsYSPSVALDYMLDGDTDRRlRGQVPRVTFLsrg 386
Cdd:pfam08441   1 RPVVSVSASLQVEPNSINPEKKNCTLTgtPVSCFTVRACFSYTGKPI-PNPSLVLNYELELDRQKK-KGLPPRVLFL--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 387 lDDLRHQSSGTVWLKHQHDRVCGDTVFQLQENVKDKLRAIVVTLSYGLRTPPlgrqAPGQELPTVAPILNAHQPSTQRTE 466
Cdd:pfam08441  76 -DSQQPSLTGTLVLLSQGRKVCRTTKAYLRDEFRDKLSPIVISLNYSLRVDP----RAPSDLPGLKPILDQNQPSTVQEQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 467 IHFLKQgCGEDKICQSNLQLErYQFCSRISDTEFqalpmdldgrtalfALSGQPFIGLELTVTNlpsdparpqaDGDDAH 546
Cdd:pfam08441 151 ANFLKD-CGEDNVCVPDLQLS-AKFDSRESDEPL--------------LLGDDNDLALEITVTN----------LGEDAY 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 547 EAQLLVTLPASLRYSGVRALDSVEKPLCLSNDSAS--HVECELGNPMKRGAQVTFYLILSTSGITIETTELEVKLLLATI 624
Cdd:pfam08441 205 EAELYVTLPPGLDYSGVRREGSEKQLSCTAKKENStrQVVCDLGNPMKRGTQVTFGLRFSVSGLELSTEELSFDLQIRST 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 625 SEQE--LDPVSVRAHVFIELPLSISGVATPQQLFFsGEVKGESAM--RSERDVGSKVKYEVTVSNQGQSlnTLGSAFLNI 700
Cdd:pfam08441 285 NEQNsnSNPVSLKVPVVAEAQLSLSGVSKPDQVVG-GSVKGESAMkpRSEEDIGPLVEHTYEVINNGPS--TVSGASLEI 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 701 MWPHEIANGKWLLYPMRVElegGQGPGKrgiCSPRPNILQLDVDSRDRRRRELGQPEPQEPPEKVEPSTSWWPVSSAekr 780
Cdd:pfam08441 362 SWPYELSNGKWLLYLLDVQ---GQGKGE---CSPQNEINPLNLTQSLESSKPLRTSRVHHVVKRRDVLKSEKATQTA--- 432

                         490
                  ....*....|....*...
gi 1720360523 781 NVTLDCAQGtAKCVVFSC 798
Cdd:pfam08441 433 SVLLSCDSG-ARCVVIRC 449
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 214-266 1.82e-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: 71.25  E-value: 1.82e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360523  214 PDSMFGISLAVLGDLNQDGFPDIAVGAPFDGD----GKVFIYHGSSLGVVVKPSQVL 266
Cdd:smart00191   1 PGSYFGYSVAGVGDVNGDGYPDLLVGAPRANDagetGAVYVYFGSSGGGNSIPLQNL 57
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 155-208 6.48e-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: 58.54  E-value: 6.48e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720360523  155 SGFGYSLA-VTDLNNDGWADLIVGAPYFFERQEelGGAVYVYMNQ--GGHWADISPL 208
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 ...
 157-195 1.65e-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: 1.65e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720360523 157 FGYSLAVTDLNNDGWADLIVGAPYFFERQeelGGAVYVY 195
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 ...
 165-238 2.47e-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: 54.15  E-value: 2.47e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720360523 165 DLNNDGWADLIVGAPyfferqeelgGAVYVYMNQG-GHWADISPLRIcgsPDSMFGISLAVlGDLNQDGFPDIAV 238
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 ...
 218-251 1.02e-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: 1.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720360523 218 FGISLAVlGDLNQDGFPDIAVGAPF---DGDGKVFIY 251
Cdd:pfam01839   1 FGYSVAV-GDLNGDGYADLAVGAPGeggAGAGAVYVL 36
FG-GAP_3 pfam13517
FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related ...
 227-296 7.79e-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: 44.14  E-value: 7.79e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720360523 227 DLNQDGFPDIAVGapfdGDGKVFIYHGSSLGVVVKPSQVlegeAVGIKSFGYSLSGGlDVDGNHYPDLLV 296
Cdd:pfam13517   1 DLDGDGKLDLVVA----NDGGLRLYLNNGDGTFTFITSV----SLGGGGGGLSVAVG-DLDGDGRLDLLV 61
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 276-316 1.23e-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: 43.52  E-value: 1.23e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1720360523  276 FGYSLSGGLDVDGNHYPDLLVGS-LADTAALFRARPVLHVSQ 316
Cdd:smart00191   5 FGYSVAGVGDVNGDGYPDLLVGApRANDAGETGAVYVYFGSS 46
Int_alpha smart00191
Integrin alpha (beta-propellor repeats); Integrins are cell adhesion molecules that mediate ...
 97-148 1.53e-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: 1.53e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720360523   97 NSYLGFSIDSGKGLMRSEELSFVAGAPRANHK---GAVVILRKDS-ASRLIPEVVL 148
Cdd:smart00191   2 GSYFGYSVAGVGDVNGDGYPDLLVGAPRANDAgetGAVYVYFGSSgGGNSIPLQNL 57
 
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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